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Botulinum neurotoxin type B (BoNT/B) (EC 3.4.24.69) (Bontoxilysin-B) [Cleaved into: Botulinum neurotoxin B light chain; Botulinum neurotoxin B heavy chain]

 BXB_CLOBO               Reviewed;        1291 AA.
P10844; P10843;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
18-JUL-2018, entry version 165.
RecName: Full=Botulinum neurotoxin type B;
Short=BoNT/B;
AltName: Full=Bontoxilysin-B;
Contains:
RecName: Full=Botulinum neurotoxin B light chain;
Short=LC;
EC=3.4.24.69 {ECO:0000269|PubMed:1331807};
Contains:
RecName: Full=Botulinum neurotoxin B heavy chain;
Short=HC;
Flags: Precursor;
Name=botB {ECO:0000303|PubMed:1514783};
Clostridium botulinum.
Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
Clostridium.
NCBI_TaxID=1491;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Danish / Type B;
PubMed=1514783;
Whelan S.M., Elmore M.J., Bodsworth N.J., Brehm J.K., Atkinson T.,
Minton N.P.;
"Molecular cloning of the Clostridium botulinum structural gene
encoding the type B neurotoxin and determination of its entire
nucleotide sequence.";
Appl. Environ. Microbiol. 58:2345-2354(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-246.
STRAIN=NCTC 7273 / Type B;
Szabo E.A., Pemberton J.M., Desmarchelier P.M.;
Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 634-994.
STRAIN=NCTC 7273 / Type B;
PubMed=8408542;
Campbell K.D., Collins M.D., East A.K.;
"Gene probes for identification of the botulinal neurotoxin gene and
specific identification of neurotoxin types B, E, and F.";
J. Clin. Microbiol. 31:2255-2262(1993).
[4]
PROTEIN SEQUENCE OF 2-45 AND 442-467, SUBUNIT, SUBCELLULAR LOCATION,
AND DISULFIDE BOND.
STRAIN=B-657 / Type B;
PubMed=3139097; DOI=10.1016/0300-9084(88)90111-3;
Dasgupta B.R., Datta A.;
"Botulinum neurotoxin type B (strain 657): partial sequence and
similarity with tetanus toxin.";
Biochimie 70:811-817(1988).
[5]
RELEASED AS SINGLE CHAIN.
STRAIN=Okra / Type B1;
PubMed=4030755;
Sathyamoorthy V., DasGupta B.R.;
"Separation, purification, partial characterization and comparison of
the heavy and light chains of botulinum neurotoxin types A, B, and
E.";
J. Biol. Chem. 260:10461-10466(1985).
[6]
FUNCTION (BOTULINUM NEUROTOXIN TYPE B AND BOTULINUM NEUROTOXIN B HEAVY
CHAIN), AND DOMAIN.
STRAIN=Type B;
PubMed=3856850;
Hoch D.H., Romero-Mira M., Ehrlich B.E., Finkelstein A.,
DasGupta B.R., Simpson L.L.;
"Channels formed by botulinum, tetanus, and diphtheria toxins in
planar lipid bilayers: relevance to translocation of proteins across
membranes.";
Proc. Natl. Acad. Sci. U.S.A. 82:1692-1696(1985).
[7]
IDENTIFICATION AS A ZINC-BINDING PROTEIN, AND COFACTOR.
STRAIN=Type B;
PubMed=1429690;
Schiavo G., Rossetto O., Santucci A., Dasgupta B.R., Montecucco C.;
"Botulinum neurotoxins are zinc proteins.";
J. Biol. Chem. 267:23479-23483(1992).
[8]
HOST RANGE, AND EPIDEMIOLOGY.
PubMed=1431246;
Woodruff B.A., Griffin P.M., McCroskey L.M., Smart J.F.,
Wainwright R.B., Bryant R.G., Hutwagner L.C., Hatheway C.L.;
"Clinical and laboratory comparison of botulism from toxin types A, B,
and E in the United States, 1975-1988.";
J. Infect. Dis. 166:1281-1286(1992).
[9]
FUNCTION (BOTULINUM NEUROTOXIN B LIGHT CHAIN), IDENTIFICATION OF
SUBSTRATE, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT, AND
SUBCELLULAR LOCATION (BOTULINUM NEUROTOXIN B LIGHT CHAIN).
STRAIN=Type B;
PubMed=1331807; DOI=10.1038/359832a0;
Schiavo G., Benfenati F., Poulain B., Rossetto O., de Laureto P.P.,
Dasgupta B.R., Montecucco C.;
"Tetanus and botulinum-B neurotoxins block neurotransmitter release by
proteolytic cleavage of synaptobrevin.";
Nature 359:832-835(1992).
[10]
FUNCTION (BOTULINUM NEUROTOXIN TYPE B), AND SUBSTRATE SPECIFICITY.
PubMed=7803399;
Foran P., Shone C.C., Dolly J.O.;
"Differences in the protease activities of tetanus and botulinum B
toxins revealed by the cleavage of vesicle-associated membrane protein
and various sized fragments.";
Biochemistry 33:15365-15374(1994).
[11]
IDENTIFICATION OF HOST RECEPTOR (BOTULINUM NEUROTOXIN TYPE B),
INTERACTION WITH HOST SYT1, AND SUBCELLULAR LOCATION (BOTULINUM
NEUROTOXIN B LIGHT CHAIN).
STRAIN=Type B;
PubMed=8144634;
Nishiki T., Kamata Y., Nemoto Y., Omori A., Ito T., Takahashi M.,
Kozaki S.;
"Identification of protein receptor for Clostridium botulinum type B
neurotoxin in rat brain synaptosomes.";
J. Biol. Chem. 269:10498-10503(1994).
[12]
FUNCTION (BOTULINUM NEUROTOXIN B HEAVY CHAIN), AND LIPID-BINDING.
STRAIN=B600 / Type B;
PubMed=10413679;
Lalli G., Herreros J., Osborne S.L., Montecucco C., Rossetto O.,
Schiavo G.;
"Functional characterisation of tetanus and botulinum neurotoxins
binding domains.";
J. Cell Sci. 112:2715-2724(1999).
[13]
RETRACTED PAPER.
PubMed=10932255; DOI=10.1038/77997;
Hanson M.A., Stevens R.C.;
"Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin
type B at 2.0 A resolution.";
Nat. Struct. Biol. 7:687-692(2000).
[14]
RETRACTION NOTICE OF PUBMED:10932255.
PubMed=19578378; DOI=10.1038/nsmb0709-795;
Hanson M.A., Stevens R.C.;
"Retraction: Cocrystal structure of synaptobrevin-II bound to
botulinum neurotoxin type B at 2.0 A resolution.";
Nat. Struct. Mol. Biol. 16:795-795(2009).
[15]
FUNCTION, IDENTIFICATION OF HOST RECEPTOR (BOTULINUM NEUROTOXIN TYPE B
AND BOTULINUM NEUROTOXIN B HEAVY CHAIN), INTERACTION WITH HOST SYT1
AND SYT2, AND SUBCELLULAR LOCATION (BOTULINUM NEUROTOXIN TYPE B).
STRAIN=Type B;
PubMed=14504267; DOI=10.1083/jcb.200305098;
Dong M., Richards D.A., Goodnough M.C., Tepp W.H., Johnson E.A.,
Chapman E.R.;
"Synaptotagmins I and II mediate entry of botulinum neurotoxin B into
cells.";
J. Cell Biol. 162:1293-1303(2003).
[16]
FUNCTION (BOTULINUM NEUROTOXIN TYPE B AND BOTULINUM NEUROTOXIN B HEAVY
CHAIN), AND INTERACTION WITH HOST SYT1 AND SYT2.
STRAIN=Type B;
PubMed=15123599; DOI=10.1074/jbc.M403945200;
Rummel A., Karnath T., Henke T., Bigalke H., Binz T.;
"Synaptotagmins I and II act as nerve cell receptors for botulinum
neurotoxin G.";
J. Biol. Chem. 279:30865-30870(2004).
[17]
FUNCTION, GANGLIOSIDE-BINDING (BOTULINUM NEUROTOXIN A HEAVY CHAIN),
AND MUTAGENESIS OF GLU-1189; GLU-1190; HIS-1241; SER-1260; TRP-1262
AND TYR-1263.
STRAIN=Okra / Type B1;
PubMed=14731268; DOI=10.1046/j.1365-2958.2003.03872.x;
Rummel A., Mahrhold S., Bigalke H., Binz T.;
"The HCC-domain of botulinum neurotoxins A and B exhibits a singular
ganglioside binding site displaying serotype specific carbohydrate
interaction.";
Mol. Microbiol. 51:631-643(2004).
[18]
DISCUSSION OF BELT FUNCTION, AND DOMAIN.
PubMed=17907800; DOI=10.1371/journal.ppat.0030113;
Brunger A.T., Breidenbach M.A., Jin R., Fischer A., Santos J.S.,
Montal M.;
"Botulinum neurotoxin heavy chain belt as an intramolecular chaperone
for the light chain.";
PLoS Pathog. 3:1191-1194(2007).
[19]
FUNCTION (BOTULINUM NEUROTOXIN TYPE B AND BOTULINUM NEUROTOXIN B HEAVY
CHAIN), INTERACTION WITH HOST SYT1 AND SYT2, AND MUTAGENESIS OF
VAL-1118; TYR-1183; GLU-1191; LYS-1192 AND TRP-1262.
STRAIN=Type B;
PubMed=17185412; DOI=10.1073/pnas.0609713104;
Rummel A., Eichner T., Weil T., Karnath T., Gutcaits A., Mahrhold S.,
Sandhoff K., Proia R.L., Acharya K.R., Bigalke H., Binz T.;
"Identification of the protein receptor binding site of botulinum
neurotoxins B and G proves the double-receptor concept.";
Proc. Natl. Acad. Sci. U.S.A. 104:359-364(2007).
[20]
FUNCTION (BOTULINUM NEUROTOXIN B HEAVY CHAIN), AND INTERACTION WITH
HOST SV2 AND SYT1.
PubMed=19476346; DOI=10.1021/bi9002138;
Fu Z., Chen C., Barbieri J.T., Kim J.J., Baldwin M.R.;
"Glycosylated SV2 and gangliosides as dual receptors for botulinum
neurotoxin serotype F.";
Biochemistry 48:5631-5641(2009).
[21]
FUNCTION (BOTULINUM NEUROTOXIN TYPE B AND BOTULINUM NEUROTOXIN B HEAVY
CHAIN), AND MUTAGENESIS OF LYS-1192 AND TRP-1262.
PubMed=19650874; DOI=10.1111/j.1471-4159.2009.06298.x;
Rummel A., Haefner K., Mahrhold S., Darashchonak N., Holt M., Jahn R.,
Beermann S., Karnath T., Bigalke H., Binz T.;
"Botulinum neurotoxins C, E and F bind gangliosides via a conserved
binding site prior to stimulation-dependent uptake with botulinum
neurotoxin F utilising the three isoforms of SV2 as second receptor.";
J. Neurochem. 110:1942-1954(2009).
[22]
FUNCTION (BOTULINUM NEUROTOXIN TYPE B AND BOTULINUM NEUROTOXIN B HEAVY
CHAIN), ENZYME REGULATION, SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=Type B;
PubMed=21925111; DOI=10.1016/j.chom.2011.06.012;
Sun S., Suresh S., Liu H., Tepp W.H., Johnson E.A., Edwardson J.M.,
Chapman E.R.;
"Receptor binding enables botulinum neurotoxin B to sense low pH for
translocation channel assembly.";
Cell Host Microbe 10:237-247(2011).
[23]
FUNCTION (BOTULINUM NEUROTOXIN TYPE B), AND SUBUNIT.
STRAIN=Type B;
PubMed=22720883; DOI=10.1021/bi3004928;
Sun S., Tepp W.H., Johnson E.A., Chapman E.R.;
"Botulinum neurotoxins B and E translocate at different rates and
exhibit divergent responses to GT1b and low pH.";
Biochemistry 51:5655-5662(2012).
[24]
FUNCTION (BOTULINUM NEUROTOXIN B LIGHT CHAIN), SUBSTRATE SPECIFICITY,
AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=22289120; DOI=10.1111/j.1348-0421.2012.00434.x;
Yamamoto H., Ida T., Tsutsuki H., Mori M., Matsumoto T., Kohda T.,
Mukamoto M., Goshima N., Kozaki S., Ihara H.;
"Specificity of botulinum protease for human VAMP family proteins.";
Microbiol. Immunol. 56:245-253(2012).
[25]
REVIEW.
PubMed=28356439; DOI=10.1124/pr.116.012658;
Pirazzini M., Rossetto O., Eleopra R., Montecucco C.;
"Botulinum neurotoxins: Biology, pharmacology, and toxicology.";
Pharmacol. Rev. 69:200-235(2017).
[26] {ECO:0000244|PDB:1EPW, ECO:0000244|PDB:1F31}
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-1291 IN COMPLEX WITH ZINC
AND GANGLIOSIDE ANALOG, FUNCTION (BOTULINUM NEUROTOXIN B HEAVY CHAIN),
COFACTOR, DOMAIN, AND GLYCAN-BINDING.
PubMed=10932256; DOI=10.1038/78005;
Swaminathan S., Eswaramoorthy S.;
"Structural analysis of the catalytic and binding sites of Clostridium
botulinum neurotoxin B.";
Nat. Struct. Biol. 7:693-699(2000).
[27] {ECO:0000244|PDB:2NM1}
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 858-1291 IN COMPLEX WITH
SYT2 RECEPTOR FRAGMENT, FUNCTION (BOTULINUM NEUROTOXIN TYPE B AND
BOTULINUM NEUROTOXIN B HEAVY CHAIN), SUBUNIT, AND MUTAGENESIS OF
VAL-1118; LYS-1192; PHE-1194; ALA-1196; SER-1199 AND PHE-1204.
STRAIN=Type B;
PubMed=17167421; DOI=10.1038/nature05387;
Jin R., Rummel A., Binz T., Brunger A.T.;
"Botulinum neurotoxin B recognizes its protein receptor with high
affinity and specificity.";
Nature 444:1092-1095(2006).
[28] {ECO:0000244|PDB:2NP0}
X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 2-1291 IN COMPLEX WITH ZINC
AND SYT2 RECEPTOR FRAGMENT, FUNCTION (BOTULINUM NEUROTOXIN TYPE B AND
BOTULINUM NEUROTOXIN B HEAVY CHAIN), COFACTOR, SUBUNIT, AND DISULFIDE
BOND.
PubMed=17167418; DOI=10.1038/nature05411;
Chai Q., Arndt J.W., Dong M., Tepp W.H., Johnson E.A., Chapman E.R.,
Stevens R.C.;
"Structural basis of cell surface receptor recognition by botulinum
neurotoxin B.";
Nature 444:1096-1100(2006).
[29] {ECO:0000244|PDB:4KBB}
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 857-1291 IN COMPLEX WITH
CORECEPTORS SYT2 AND GANGLIOSIDE GD1A, FUNCTION (BOTULINUM NEUROTOXIN
B HEAVY CHAIN), AND SUBUNIT.
STRAIN=Okra / Type B1;
PubMed=23807078; DOI=10.1038/ncomms3058;
Berntsson R.P., Peng L., Dong M., Stenmark P.;
"Structure of dual receptor binding to botulinum neurotoxin B.";
Nat. Commun. 4:2058-2058(2013).
-!- FUNCTION: Botulinum neurotoxin type B: Botulinum toxin causes
flaccid paralysis by inhibiting neurotransmitter (acetylcholine)
release from the presynaptic membranes of nerve terminals of the
eukaryotic host skeletal and autonomic nervous system, with
frequent heart or respiratory failure. Precursor of botulinum
neurotoxin B which has 2 coreceptors; complex polysialylated
gangliosides found on neural tissue and specific membrane-anchored
proteins found in synaptic vesicles (PubMed:17185412,
PubMed:17167421, PubMed:17167418, PubMed:23807078). Receptor
proteins are exposed on host presynaptic cell membrane during
neurotransmitter release, when the toxin heavy chain (HC) binds to
them (PubMed:14504267). Upon synaptic vesicle recycling the toxin
is taken up via the endocytic pathway (PubMed:14504267). When the
pH of the toxin-containing endosome drops a structural
rearrangement occurs so that the N-terminus of the HC forms pores
that allows the light chain (LC) to translocate into the cytosol
(PubMed:3856850). Once in the cytosol the disulfide bond linking
the 2 subunits is reduced and LC cleaves its target protein on
synaptic vesicles, preventing their fusion with the cytoplasmic
membrane and thus neurotransmitter release. Binds to host
peripheral neuronal presynaptic membranes via synaptotagmins 1 and
2 (SYT1 and SYT2) (PubMed:8144634, PubMed:14504267). Toxin binds
to the membrane proximal extra-cytoplasmic region of host SYT1 and
SYT2 that is transiently exposed outside of cells during
exocytosis; exogenous gangliosides enhance binding and subsequent
uptake of toxin into host cells (PubMed:14504267,
PubMed:15123599). Toxin uptake into neural cells requires
stimulation (incubation with K(+) to stimulate SYT protein
receptor exposure); subsequently the toxin colocalizes with its
receptor in host cells with a concomitant decrease in target
protein (synaptobrevin-2/VAMP2) immunoreactivity
(PubMed:14504267). Toxin uptake can be blocked by the appropriate
synaptotagmin protein fragments and gangliosides in cell culture
and in mice (PubMed:14504267, PubMed:15123599). BoNT/B is a
'coincidence detector'; it requires simultaneous binding to
coreceptor GT1b and low pH to transform into a membrane-bound,
oligomeric channel (PubMed:21925111, PubMed:22720883). Whole toxin
only has protease activity after reduction which releases LC
(PubMed:1331807, PubMed:7803399). {ECO:0000269|PubMed:1331807,
ECO:0000269|PubMed:14504267, ECO:0000269|PubMed:15123599,
ECO:0000269|PubMed:17167418, ECO:0000269|PubMed:17167421,
ECO:0000269|PubMed:17185412, ECO:0000269|PubMed:21925111,
ECO:0000269|PubMed:22720883, ECO:0000269|PubMed:23807078,
ECO:0000269|PubMed:3856850, ECO:0000269|PubMed:7803399,
ECO:0000269|PubMed:8144634}.
-!- FUNCTION: Botulinum neurotoxin B light chain: Has proteolytic
activity (PubMed:1331807). After translocation into the eukaryotic
host cytosol, inhibits neurotransmitter release by acting as a
zinc endopeptidase that cleaves the '76-Gln-|-Phe-77' bond of
synaptobrevin-2/VAMP2, blocking neurotransmitter release
(PubMed:1331807, PubMed:7803399). In vitro the LC only has
protease activity after reduction (PubMed:1331807,
PubMed:7803399). {ECO:0000269|PubMed:1331807,
ECO:0000305|PubMed:7803399}.
-!- FUNCTION: Botulinum neurotoxin B heavy chain: Responsible for host
epithelial cell transcytosis, host nerve cell targeting and
translocation of light chain (LC) into host cytosol. Composed of 3
subdomains; the translocation domain (TD), and N-terminus and C-
terminus of the receptor-binding domain (RBD). The N-terminus of
the TD wraps an extended belt around the perimeter of the LC; it
does not seem to protect the active site, but might prevent
premature LC dissociation from the translocation channel and
protect toxin prior to translocation (PubMed:10932256,
PubMed:17167418). Has 2 coreceptors; complex gangliosides found
primarily on neural tissue and host synaptotagmin-1 and -2 (SYT1
and SYT2) which bind simultaneously to adjacent but separate sites
at the tip of the HC (PubMed:8144634, PubMed:17185412,
PubMed:17167421, PubMed:17167418, PubMed:23807078). HC alone
partially prevents uptake of whole toxin by neural cells, and
delays paralysis onset by 160% (PubMed:10413679). Binding probably
positions the TD for integration into the synaptic vesicle
membrane (PubMed:17167418, PubMed:23807078). The HC forms channels
at low pH that mediate transport of the light chain (LC) from the
endocytic vesicle to the cytosol (PubMed:3856850). Binds
gangliosides GD1b and GT1b (PubMed:10413679, PubMed:14731268).
Gangliosides are not only a coreceptor, but also required for
uptake into nerve cells (PubMed:21925111, PubMed:17167418). HC
alone binds to host receptor proteins SYT1 and SYT2
(PubMed:14504267, PubMed:15123599, PubMed:17185412). Interaction
with SYT1 protein does not requires SYT1 glycosylation
(PubMed:19476346). The HC C-terminus (approximately residues 1079-
1291) interacts with host SYT2 (PubMed:15123599, PubMed:17167421,
PubMed:17167418, PubMed:23807078). Has higher affinity for SYT2
than SYT1 (PubMed:17185412, PubMed:17167421). Significantly
decreases uptake and toxicity of whole BoNT/B and BoNT/G
(PubMed:19650874). {ECO:0000269|PubMed:10413679,
ECO:0000269|PubMed:10932256, ECO:0000269|PubMed:14504267,
ECO:0000269|PubMed:14731268, ECO:0000269|PubMed:15123599,
ECO:0000269|PubMed:17167418, ECO:0000269|PubMed:17167421,
ECO:0000269|PubMed:17185412, ECO:0000269|PubMed:19650874,
ECO:0000269|PubMed:23807078, ECO:0000269|PubMed:8144634,
ECO:0000305|PubMed:21925111, ECO:0000305|PubMed:3856850}.
-!- CATALYTIC ACTIVITY: Limited hydrolysis of proteins of the
neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No
detected action on small molecule substrates.
{ECO:0000269|PubMed:1331807}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:10932256,
ECO:0000269|PubMed:1429690, ECO:0000269|PubMed:17167418};
Note=Binds 1 zinc ion per subunit, to the LC (PubMed:1429690,
PubMed:10932256, PubMed:17167418). {ECO:0000269|PubMed:10932256,
ECO:0000269|PubMed:1429690, ECO:0000269|PubMed:17167418};
-!- ENZYME REGULATION: Proteolysis inhibited by EDTA and captopril,
and by peptides that encompass the VAMP2 cleavage site (Ala-Ser-
Gln-Phe-Glu-Thr-Ser and Gln-Phe-Glu-Thr) (PubMed:1331807).
Translocation of whole toxin into neurons is inhibited by
toosendanin (PubMed:21925111). {ECO:0000269|PubMed:1331807,
ECO:0000269|PubMed:21925111}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=19.2 uM for over-expressed human VAMP1
{ECO:0000269|PubMed:22289120};
KM=29.9 uM for over-expressed human VAMP2
{ECO:0000269|PubMed:22289120};
KM=11.6 uM for over-expressed human VAMP3
{ECO:0000269|PubMed:22289120};
Note=kcat is 3.96, 4.68 and 3.50 s(-1) for over-expressed human
VAMP1, VAMP2 and VAMP3 respectively.
{ECO:0000269|PubMed:22289120};
-!- SUBUNIT: Heterodimer; disulfide-linked heterodimer of a light
chain (LC) and a heavy chain (HC) (PubMed:3139097,
PubMed:1331807). At pH 4.4 in the presence of ganglioside GT1b may
form trimers (PubMed:21925111, PubMed:22720883). Interacts with
host receptor synaptotagmin-1 (SYT1); interaction is improved in
the presence of gangliosides (PubMed:8144634, PubMed:14504267).
Interacts with host receptor synaptotagmin-2 (SYT2)
(PubMed:14504267, PubMed:15123599, PubMed:17167421,
PubMed:17167418, PubMed:23807078). SYT2 interaction and toxin
uptake do not require gangliosides but are improved in their
presence (PubMed:14504267, PubMed:15123599). HC interacts with a
complex including at least host synaptic vesicle glycoprotein 2
(SV2) and synaptotagmin-1 (SYT1); copurification does not depend
on glycosylation of either protein (PubMed:19476346).
{ECO:0000269|PubMed:1331807, ECO:0000269|PubMed:14504267,
ECO:0000269|PubMed:15123599, ECO:0000269|PubMed:17167418,
ECO:0000269|PubMed:17167421, ECO:0000269|PubMed:19476346,
ECO:0000269|PubMed:21925111, ECO:0000269|PubMed:22720883,
ECO:0000269|PubMed:23807078, ECO:0000269|PubMed:3139097,
ECO:0000269|PubMed:8144634}.
-!- INTERACTION:
P29101:Syt2 (xeno); NbExp=6; IntAct=EBI-7661991, EBI-458017;
P46097:Syt2 (xeno); NbExp=3; IntAct=EBI-7661991, EBI-457969;
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin type B: Secreted
{ECO:0000269|PubMed:3139097}. Host cell junction, host synapse,
host presynaptic cell membrane {ECO:0000269|PubMed:14504267}.
Note=Colocalizes with its SYT1 receptor, probably in synaptic
vesicles (PubMed:14504267). At pH 4.4 in the presence of
ganglioside GT1b becomes a membrane-associated hydrophobic protein
(PubMed:21925111). {ECO:0000269|PubMed:14504267,
ECO:0000269|PubMed:21925111}.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin B light chain: Secreted
{ECO:0000269|PubMed:3139097}. Host cytoplasm, host cytosol
{ECO:0000305|PubMed:1331807, ECO:0000305|PubMed:8144634}.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin B heavy chain: Secreted
{ECO:0000269|PubMed:3139097}. Host cell junction, host synapse,
host presynaptic cell membrane {ECO:0000269|PubMed:14504267}. Host
cytoplasmic vesicle, host secretory vesicle, host synaptic vesicle
membrane {ECO:0000305|PubMed:21925111}; Multi-pass membrane
protein {ECO:0000305}.
-!- DOMAIN: Botulinum neurotoxin B light chain: Has protease activity
(PubMed:1331807). {ECO:0000269|PubMed:1331807}.
-!- DOMAIN: Botulinum neurotoxin B heavy chain: Has 3 functional
domains; the translocation domain (TD) and the receptor-binding
domain (RBD) which is further subdivided into N- and C-terminal
domains (N-RBD and C-RBD) (PubMed:10932256). HC forms channels in
bilayers at low pH (PubMed:3856850). The N-terminal belt of the TD
wraps an extended belt around the perimeter of the LC; it is
shorter than in BoNT/A and does not block the active site
(PubMed:10932256). The belt may be a pseudosubstrate inhibitor
which serves as an intramolecular chaperone for the LC prior to
its translocation into the host cytosol (PubMed:17907800).
{ECO:0000269|PubMed:10932256, ECO:0000269|PubMed:3856850,
ECO:0000305|PubMed:17907800}.
-!- PHARMACEUTICAL: Available under the name MYOBLOC
(rimabotulinumtoxinB, US WorldMeds, LLC) for the treatment of
adults with cervical dystonia.
-!- MISCELLANEOUS: There are seven antigenically distinct forms of
botulinum neurotoxin: Types A, B, C, D, E, F, and G; new subtypes
are quite frequent.
-!- MISCELLANEOUS: Botulism poisoning is usually food-borne, either by
ingesting toxin or bacterial-contaminated food, or less frequently
by inhalation poisoning. In both cases the neurotoxin binds to the
apical surface of epithelial cells in the gut or airway. Toxin
undergoes receptor-mediated endocytosis (using a different
receptor than on target nerve cells), transcytosis across the
epithelial cells and release into the general circulation. Once in
the general circulation it binds to its target cells.
{ECO:0000250|UniProtKB:P0DPI0}.
-!- MISCELLANEOUS: Types A, B and E are the most frequent cause of
adult human foodborne botulism; type A is the most severe, while
type E has the shortest incubation period (PubMed:1431246).
{ECO:0000269|PubMed:1431246}.
-!- MISCELLANEOUS: Neurotoxin type B is released from bacteria mostly
as a single chain and cleaved by host proteases into the active
dichain (PubMed:4030755). {ECO:0000269|PubMed:4030755}.
-!- SIMILARITY: Belongs to the peptidase M27 family. {ECO:0000305}.
-!- CAUTION: A structure of a fragment of this protein in complex with
the catalytic domain of C.botulinum neurotoxin type B (BoNT/B,
botB) was reported; because of the lack of clear and continuous
electron density for the VAMP2 peptide in the complex structure,
the paper was retracted. One of its associated structures remains
valid (PDB:1F82, light chain alone) (PubMed:10932255,
PubMed:19578378). {ECO:0000269|PubMed:10932255,
ECO:0000269|PubMed:19578378}.
-!- WEB RESOURCE: Name=BotDB - A Database Resource for Clostridial
Neurotoxins;
URL="https://botdb.abcc.ncifcrf.gov/";
-----------------------------------------------------------------------
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EMBL; M81186; AAA23211.1; -; Genomic_DNA.
EMBL; Z11934; CAA77991.1; -; Genomic_DNA.
EMBL; X70817; CAA50148.1; -; Genomic_DNA.
PIR; A48940; A48940.
PDB; 1EPW; X-ray; 1.90 A; A=2-1291.
PDB; 1F31; X-ray; 2.60 A; A=2-1291.
PDB; 1F82; X-ray; 2.20 A; A=2-425.
PDB; 1G9A; X-ray; 2.10 A; A=2-1291.
PDB; 1G9B; X-ray; 2.00 A; A=2-1291.
PDB; 1G9C; X-ray; 2.35 A; A=2-1291.
PDB; 1G9D; X-ray; 2.20 A; A=2-1291.
PDB; 1I1E; X-ray; 2.50 A; A=2-1291.
PDB; 1S0B; X-ray; 2.00 A; A=2-1291.
PDB; 1S0C; X-ray; 2.20 A; A=2-1291.
PDB; 1S0D; X-ray; 2.20 A; A=2-1291.
PDB; 1S0E; X-ray; 1.90 A; A=2-1291.
PDB; 1S0F; X-ray; 2.30 A; A=2-1291.
PDB; 1S0G; X-ray; 2.60 A; A=2-1291.
PDB; 1Z0H; X-ray; 2.00 A; A/B=854-1291.
PDB; 2ETF; X-ray; 2.29 A; A/B=1-441.
PDB; 2NM1; X-ray; 2.15 A; A=858-1291.
PDB; 2NP0; X-ray; 2.62 A; A=2-1291.
PDB; 2XHL; X-ray; 2.80 A; A=1-437, B=446-858.
PDB; 3ZUQ; X-ray; 2.70 A; A=1-437, A=446-858.
PDB; 4KBB; X-ray; 2.30 A; A/B=857-1291.
PDB; 5VID; X-ray; 2.75 A; A/B/C/D/E=859-1291.
PDB; 5VMR; X-ray; 1.95 A; A/B=859-1291.
PDBsum; 1EPW; -.
PDBsum; 1F31; -.
PDBsum; 1F82; -.
PDBsum; 1G9A; -.
PDBsum; 1G9B; -.
PDBsum; 1G9C; -.
PDBsum; 1G9D; -.
PDBsum; 1I1E; -.
PDBsum; 1S0B; -.
PDBsum; 1S0C; -.
PDBsum; 1S0D; -.
PDBsum; 1S0E; -.
PDBsum; 1S0F; -.
PDBsum; 1S0G; -.
PDBsum; 1Z0H; -.
PDBsum; 2ETF; -.
PDBsum; 2NM1; -.
PDBsum; 2NP0; -.
PDBsum; 2XHL; -.
PDBsum; 3ZUQ; -.
PDBsum; 4KBB; -.
PDBsum; 5VID; -.
PDBsum; 5VMR; -.
ProteinModelPortal; P10844; -.
SMR; P10844; -.
DIP; DIP-42782N; -.
IntAct; P10844; 4.
MINT; P10844; -.
BindingDB; P10844; -.
ChEMBL; CHEMBL1075064; -.
DrugBank; DB02379; Beta-D-Glucose.
DrugBank; DB01705; Bis(5-Amidino-Benzimidazolyl)Methane.
DrugBank; DB03721; N-acetyl-alpha-neuraminic acid.
MEROPS; M27.002; -.
UniLectin; P10844; -.
BRENDA; 3.4.24.69; 1462.
Reactome; R-HSA-5250958; Toxicity of botulinum toxin type B (BoNT/B).
EvolutionaryTrace; P10844; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044164; C:host cell cytosol; IEA:UniProtKB-SubCell.
GO; GO:0044156; C:host cell junction; IEA:UniProtKB-KW.
GO; GO:0044231; C:host cell presynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; EXP:Reactome.
GO; GO:0008320; F:protein transmembrane transporter activity; EXP:Reactome.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0046929; P:negative regulation of neurotransmitter secretion; IEA:InterPro.
Gene3D; 1.20.1120.10; -; 2.
InterPro; IPR000395; Bot/tetX_LC.
InterPro; IPR036248; Clostridium_toxin_transloc.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
InterPro; IPR013104; Toxin_rcpt-bd_C.
InterPro; IPR012928; Toxin_rcpt-bd_N.
InterPro; IPR012500; Toxin_trans.
Pfam; PF01742; Peptidase_M27; 1.
Pfam; PF07951; Toxin_R_bind_C; 1.
Pfam; PF07953; Toxin_R_bind_N; 1.
Pfam; PF07952; Toxin_trans; 1.
PRINTS; PR00760; BONTOXILYSIN.
SUPFAM; SSF49899; SSF49899; 1.
SUPFAM; SSF50386; SSF50386; 1.
SUPFAM; SSF58091; SSF58091; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Disulfide bond;
Host cell junction; Host cell membrane; Host cytoplasm;
Host cytoplasmic vesicle; Host membrane; Host synapse; Hydrolase;
Lipid-binding; Membrane; Metal-binding; Metalloprotease; Neurotoxin;
Pharmaceutical; Protease; Secreted; Toxin; Transmembrane; Virulence;
Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:3139097}.
CHAIN 2 1291 Botulinum neurotoxin type B.
/FTId=PRO_0000444904.
CHAIN 2 441 Botulinum neurotoxin B light chain.
/FTId=PRO_0000029215.
CHAIN 442 1291 Botulinum neurotoxin B heavy chain.
/FTId=PRO_0000029216.
REGION 442 857 Translocation domain (TD).
{ECO:0000250|UniProtKB:P0DPI0}.
REGION 481 532 Belt; not required for channel formation.
{ECO:0000305|PubMed:10932256}.
REGION 858 1079 N-terminus of receptor binding domain (N-
RBD). {ECO:0000250|UniProtKB:P0DPI0}.
REGION 1080 1291 C-terminus of receptor binding domain (C-
RBD). {ECO:0000250|UniProtKB:P0DPI0}.
REGION 1189 1190 Host ganglioside GT1b binding.
{ECO:0000244|PDB:4KBB,
ECO:0000269|PubMed:10932256,
ECO:0000305|PubMed:14731268}.
REGION 1240 1241 Galactose binding. {ECO:0000244|PDB:4KBB,
ECO:0000269|PubMed:10932256,
ECO:0000305|PubMed:14731268}.
MOTIF 1260 1263 Host ganglioside-binding motif.
{ECO:0000269|PubMed:10932256,
ECO:0000305|PubMed:14731268,
ECO:0000305|PubMed:17185412}.
ACT_SITE 231 231 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 230 230 Zinc; via tele nitrogen; catalytic.
{ECO:0000244|PDB:1EPW,
ECO:0000244|PDB:1F31,
ECO:0000244|PDB:2NP0,
ECO:0000255|PROSITE-ProRule:PRU10095,
ECO:0000269|PubMed:10932256,
ECO:0000305|PubMed:1429690}.
METAL 234 234 Zinc; via tele nitrogen; catalytic.
{ECO:0000244|PDB:1EPW,
ECO:0000244|PDB:1F31,
ECO:0000244|PDB:2NP0,
ECO:0000255|PROSITE-ProRule:PRU10095,
ECO:0000269|PubMed:10932256,
ECO:0000305|PubMed:1429690}.
METAL 268 268 Zinc; catalytic. {ECO:0000244|PDB:1EPW,
ECO:0000244|PDB:1F31,
ECO:0000244|PDB:2NP0,
ECO:0000269|PubMed:10932256}.
BINDING 1025 1025 Host ganglioside GT1b binding; via amide
nitrogen. {ECO:0000244|PDB:4KBB}.
DISULFID 437 446 Interchain (between light and heavy
chains). {ECO:0000244|PDB:1EPW,
ECO:0000244|PDB:1F31,
ECO:0000244|PDB:2NP0,
ECO:0000269|PubMed:10932256,
ECO:0000269|PubMed:17167418,
ECO:0000305|PubMed:3139097}.
MUTAGEN 1118 1118 V->D: Greatly decreased binding of heavy
chain (HC) to host SYT2, whole toxin
about 200-fold less toxic. Significantly
decreased binding of HC to host SYT1 and
SYT2 independent of gangliosides; whole
toxin about 100-fold less toxic.
{ECO:0000269|PubMed:17167421,
ECO:0000269|PubMed:17185412}.
MUTAGEN 1183 1183 Y->R: Significantly decreased binding of
heavy chain to host SYT1 and SYT2
independent of gangliosides.
{ECO:0000269|PubMed:17185412}.
MUTAGEN 1189 1189 E->L: Decreased toxicity, heavy chain has
decreased binding to synaptosomes and to
GT1b. {ECO:0000269|PubMed:14731268}.
MUTAGEN 1190 1190 E->L: Greatly decreased toxicity, heavy
chain has decreased binding to
synaptosomes, binds less GT1b.
{ECO:0000269|PubMed:14731268}.
MUTAGEN 1191 1191 E->L: Increased binding of heavy chain to
host SYT1, no effect on binding to SYT2
independent of gangliosides.
{ECO:0000269|PubMed:17185412}.
MUTAGEN 1192 1192 K->E: Greatly decreased binding of heavy
chain to host SYT2, whole toxin about
dramatically less toxic. Significantly
decreased binding of heavy chain to host
SYT1 and SYT2 independent of
gangliosides; whole toxin significantly
less toxic. Essentially non-toxic; when
associated with L-1262. Heavy chain no
longer inhibits whole-toxin uptake and
toxicity. {ECO:0000269|PubMed:17167421,
ECO:0000269|PubMed:17185412,
ECO:0000269|PubMed:19650874}.
MUTAGEN 1192 1192 K->M,Y: Decreased binding of heavy chain
to host SYT1 and SYT2 independent of
gangliosides.
{ECO:0000269|PubMed:17185412}.
MUTAGEN 1194 1194 F->A: Greatly decreased binding of heavy
chain to host SYT2, whole toxin about 40-
fold less toxic.
{ECO:0000269|PubMed:17167421}.
MUTAGEN 1196 1196 A->K: Greatly decreased binding of heavy
chain to host SYT2, whole toxin about
1000-fold less toxic.
{ECO:0000269|PubMed:17167421}.
MUTAGEN 1199 1199 S->Y: Increased binding of heavy chain to
host SYT2, no effect on toxicity.
{ECO:0000269|PubMed:17167421}.
MUTAGEN 1204 1204 F->A: Greatly decreased binding of heavy
chain to host SYT2, whole toxin about 30-
fold less toxic.
{ECO:0000269|PubMed:17167421}.
MUTAGEN 1241 1241 H->A: Decreased toxicity, heavy chain has
decreased binding to synaptosomes and to
GT1b. {ECO:0000269|PubMed:14731268}.
MUTAGEN 1241 1241 H->W: Greatly decreased toxicity, heavy
chain has decreased binding to
synaptosomes and dramatic decrease in
GT1b binding.
{ECO:0000269|PubMed:14731268}.
MUTAGEN 1260 1260 S->A: Greatly decreased toxicity, heavy
chain has decreased binding to
synaptosome and binds less GT1b.
{ECO:0000269|PubMed:14731268}.
MUTAGEN 1262 1262 W->L: Greatly decreased toxicity, heavy
chain has decreased binding to
synaptosomes, heavy chain has dramatic
decrease in GT1b binding. Gangliosides no
longer increase heavy chain affinity for
SYT1 or SYT2; whole toxin significantly
less toxic. Essentially non-toxic; when
associated with E-1192. Heavy chain no
longer inhibits whole-toxin uptake and
toxicity. In mice without complex
gangliosides no change compared to wild-
type protein.
{ECO:0000269|PubMed:14731268,
ECO:0000269|PubMed:17185412,
ECO:0000269|PubMed:19650874}.
MUTAGEN 1263 1263 Y->F: Greatly decreased toxicity, heavy
chain has intermediate binding to
synaptosomes, binds less GT1b.
{ECO:0000269|PubMed:14731268}.
MUTAGEN 1263 1263 Y->S: Greatly decreased toxicity, heavy
chain has decreased binding to
synaptosomes and dramatic decrease in
GT1b binding.
{ECO:0000269|PubMed:14731268}.
CONFLICT 30 30 T -> M (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 218 218 R -> G (in Ref. 2; CAA77991).
{ECO:0000305}.
CONFLICT 225 225 A -> S (in Ref. 2; CAA77991).
{ECO:0000305}.
CONFLICT 464 464 S -> R (in Ref. 4; AA sequence).
{ECO:0000305}.
STRAND 16 23 {ECO:0000244|PDB:1EPW}.
HELIX 25 27 {ECO:0000244|PDB:1EPW}.
TURN 28 31 {ECO:0000244|PDB:1F82}.
STRAND 34 40 {ECO:0000244|PDB:1EPW}.
STRAND 43 46 {ECO:0000244|PDB:1EPW}.
HELIX 56 59 {ECO:0000244|PDB:1EPW}.
STRAND 63 66 {ECO:0000244|PDB:1EPW}.
STRAND 72 74 {ECO:0000244|PDB:1EPW}.
TURN 76 79 {ECO:0000244|PDB:1EPW}.
HELIX 82 99 {ECO:0000244|PDB:1EPW}.
HELIX 103 114 {ECO:0000244|PDB:1EPW}.
STRAND 122 124 {ECO:0000244|PDB:1G9D}.
TURN 134 136 {ECO:0000244|PDB:1EPW}.
STRAND 137 141 {ECO:0000244|PDB:1EPW}.
STRAND 145 148 {ECO:0000244|PDB:1F82}.
STRAND 151 155 {ECO:0000244|PDB:1EPW}.
STRAND 157 161 {ECO:0000244|PDB:1EPW}.
STRAND 171 173 {ECO:0000244|PDB:1EPW}.
STRAND 176 179 {ECO:0000244|PDB:1G9D}.
HELIX 182 184 {ECO:0000244|PDB:1EPW}.
STRAND 185 187 {ECO:0000244|PDB:1EPW}.
STRAND 191 194 {ECO:0000244|PDB:1EPW}.
STRAND 197 203 {ECO:0000244|PDB:1EPW}.
STRAND 206 208 {ECO:0000244|PDB:1G9B}.
STRAND 210 212 {ECO:0000244|PDB:1S0E}.
STRAND 214 216 {ECO:0000244|PDB:1EPW}.
STRAND 219 221 {ECO:0000244|PDB:1EPW}.
HELIX 224 239 {ECO:0000244|PDB:1EPW}.
HELIX 266 272 {ECO:0000244|PDB:1EPW}.
HELIX 276 279 {ECO:0000244|PDB:1EPW}.
HELIX 282 305 {ECO:0000244|PDB:1EPW}.
STRAND 308 311 {ECO:0000244|PDB:1EPW}.
HELIX 317 327 {ECO:0000244|PDB:1EPW}.
STRAND 330 332 {ECO:0000244|PDB:1F82}.
STRAND 338 340 {ECO:0000244|PDB:1F82}.
HELIX 342 354 {ECO:0000244|PDB:1EPW}.
HELIX 358 365 {ECO:0000244|PDB:1EPW}.
STRAND 373 375 {ECO:0000244|PDB:1EPW}.
STRAND 378 384 {ECO:0000244|PDB:1EPW}.
TURN 389 391 {ECO:0000244|PDB:1EPW}.
TURN 394 396 {ECO:0000244|PDB:1EPW}.
HELIX 401 403 {ECO:0000244|PDB:1EPW}.
HELIX 407 412 {ECO:0000244|PDB:1EPW}.
TURN 414 416 {ECO:0000244|PDB:1EPW}.
HELIX 418 420 {ECO:0000244|PDB:1EPW}.
STRAND 421 423 {ECO:0000244|PDB:1S0E}.
HELIX 426 428 {ECO:0000244|PDB:1EPW}.
STRAND 433 437 {ECO:0000244|PDB:1EPW}.
STRAND 446 450 {ECO:0000244|PDB:1EPW}.
HELIX 451 453 {ECO:0000244|PDB:1EPW}.
HELIX 460 462 {ECO:0000244|PDB:1EPW}.
HELIX 466 468 {ECO:0000244|PDB:1EPW}.
STRAND 471 473 {ECO:0000244|PDB:1EPW}.
HELIX 488 493 {ECO:0000244|PDB:1EPW}.
STRAND 495 498 {ECO:0000244|PDB:1EPW}.
STRAND 506 508 {ECO:0000244|PDB:1EPW}.
STRAND 524 531 {ECO:0000244|PDB:1EPW}.
HELIX 537 542 {ECO:0000244|PDB:1EPW}.
STRAND 554 557 {ECO:0000244|PDB:1EPW}.
HELIX 559 564 {ECO:0000244|PDB:1EPW}.
STRAND 568 570 {ECO:0000244|PDB:1EPW}.
HELIX 575 581 {ECO:0000244|PDB:1EPW}.
HELIX 587 606 {ECO:0000244|PDB:1EPW}.
HELIX 607 609 {ECO:0000244|PDB:1EPW}.
STRAND 610 612 {ECO:0000244|PDB:1G9B}.
HELIX 613 615 {ECO:0000244|PDB:1EPW}.
STRAND 617 620 {ECO:0000244|PDB:1G9B}.
HELIX 624 628 {ECO:0000244|PDB:1EPW}.
TURN 631 635 {ECO:0000244|PDB:1EPW}.
HELIX 639 646 {ECO:0000244|PDB:1EPW}.
HELIX 647 651 {ECO:0000244|PDB:1EPW}.
STRAND 666 668 {ECO:0000244|PDB:1EPW}.
HELIX 675 707 {ECO:0000244|PDB:1EPW}.
HELIX 709 738 {ECO:0000244|PDB:1EPW}.
HELIX 743 747 {ECO:0000244|PDB:1EPW}.
HELIX 753 786 {ECO:0000244|PDB:1EPW}.
HELIX 788 812 {ECO:0000244|PDB:1EPW}.
HELIX 814 817 {ECO:0000244|PDB:1EPW}.
TURN 819 824 {ECO:0000244|PDB:1EPW}.
HELIX 825 831 {ECO:0000244|PDB:1EPW}.
HELIX 840 842 {ECO:0000244|PDB:1EPW}.
HELIX 847 857 {ECO:0000244|PDB:1EPW}.
HELIX 860 863 {ECO:0000244|PDB:1EPW}.
STRAND 864 870 {ECO:0000244|PDB:1EPW}.
STRAND 872 877 {ECO:0000244|PDB:1EPW}.
STRAND 879 881 {ECO:0000244|PDB:1EPW}.
STRAND 884 887 {ECO:0000244|PDB:1EPW}.
STRAND 891 893 {ECO:0000244|PDB:5VMR}.
STRAND 897 901 {ECO:0000244|PDB:1EPW}.
STRAND 909 912 {ECO:0000244|PDB:1EPW}.
TURN 915 917 {ECO:0000244|PDB:2NP0}.
STRAND 918 923 {ECO:0000244|PDB:5VMR}.
STRAND 926 933 {ECO:0000244|PDB:1EPW}.
HELIX 939 941 {ECO:0000244|PDB:1EPW}.
HELIX 942 947 {ECO:0000244|PDB:1EPW}.
STRAND 949 957 {ECO:0000244|PDB:1EPW}.
STRAND 960 967 {ECO:0000244|PDB:1EPW}.
STRAND 970 976 {ECO:0000244|PDB:1EPW}.
STRAND 978 980 {ECO:0000244|PDB:1S0F}.
STRAND 982 988 {ECO:0000244|PDB:1EPW}.
STRAND 991 995 {ECO:0000244|PDB:2NM1}.
STRAND 1003 1009 {ECO:0000244|PDB:1EPW}.
STRAND 1011 1018 {ECO:0000244|PDB:1EPW}.
STRAND 1021 1027 {ECO:0000244|PDB:1EPW}.
STRAND 1038 1047 {ECO:0000244|PDB:1EPW}.
STRAND 1054 1064 {ECO:0000244|PDB:1EPW}.
HELIX 1068 1079 {ECO:0000244|PDB:1EPW}.
STRAND 1089 1091 {ECO:0000244|PDB:1EPW}.
STRAND 1093 1095 {ECO:0000244|PDB:1Z0H}.
STRAND 1097 1102 {ECO:0000244|PDB:1EPW}.
HELIX 1103 1105 {ECO:0000244|PDB:1Z0H}.
STRAND 1108 1112 {ECO:0000244|PDB:1EPW}.
STRAND 1116 1123 {ECO:0000244|PDB:1EPW}.
STRAND 1145 1149 {ECO:0000244|PDB:1EPW}.
TURN 1153 1155 {ECO:0000244|PDB:1S0G}.
STRAND 1166 1173 {ECO:0000244|PDB:1EPW}.
STRAND 1176 1183 {ECO:0000244|PDB:1EPW}.
STRAND 1188 1192 {ECO:0000244|PDB:1EPW}.
STRAND 1194 1198 {ECO:0000244|PDB:1EPW}.
STRAND 1202 1205 {ECO:0000244|PDB:5VMR}.
STRAND 1208 1211 {ECO:0000244|PDB:1EPW}.
STRAND 1215 1217 {ECO:0000244|PDB:5VID}.
STRAND 1221 1231 {ECO:0000244|PDB:1EPW}.
STRAND 1234 1246 {ECO:0000244|PDB:1EPW}.
STRAND 1248 1250 {ECO:0000244|PDB:2NM1}.
STRAND 1251 1260 {ECO:0000244|PDB:1EPW}.
HELIX 1263 1266 {ECO:0000244|PDB:1EPW}.
STRAND 1269 1271 {ECO:0000244|PDB:1EPW}.
STRAND 1280 1283 {ECO:0000244|PDB:1EPW}.
SEQUENCE 1291 AA; 150803 MW; 921DE5C518140DBD CRC64;
MPVTINNFNY NDPIDNNNII MMEPPFARGT GRYYKAFKIT DRIWIIPERY TFGYKPEDFN
KSSGIFNRDV CEYYDPDYLN TNDKKNIFLQ TMIKLFNRIK SKPLGEKLLE MIINGIPYLG
DRRVPLEEFN TNIASVTVNK LISNPGEVER KKGIFANLII FGPGPVLNEN ETIDIGIQNH
FASREGFGGI MQMKFCPEYV SVFNNVQENK GASIFNRRGY FSDPALILMH ELIHVLHGLY
GIKVDDLPIV PNEKKFFMQS TDAIQAEELY TFGGQDPSII TPSTDKSIYD KVLQNFRGIV
DRLNKVLVCI SDPNININIY KNKFKDKYKF VEDSEGKYSI DVESFDKLYK SLMFGFTETN
IAENYKIKTR ASYFSDSLPP VKIKNLLDNE IYTIEEGFNI SDKDMEKEYR GQNKAINKQA
YEEISKEHLA VYKIQMCKSV KAPGICIDVD NEDLFFIADK NSFSDDLSKN ERIEYNTQSN
YIENDFPINE LILDTDLISK IELPSENTES LTDFNVDVPV YEKQPAIKKI FTDENTIFQY
LYSQTFPLDI RDISLTSSFD DALLFSNKVY SFFSMDYIKT ANKVVEAGLF AGWVKQIVND
FVIEANKSNT MDKIADISLI VPYIGLALNV GNETAKGNFE NAFEIAGASI LLEFIPELLI
PVVGAFLLES YIDNKNKIIK TIDNALTKRN EKWSDMYGLI VAQWLSTVNT QFYTIKEGMY
KALNYQAQAL EEIIKYRYNI YSEKEKSNIN IDFNDINSKL NEGINQAIDN INNFINGCSV
SYLMKKMIPL AVEKLLDFDN TLKKNLLNYI DENKLYLIGS AEYEKSKVNK YLKTIMPFDL
SIYTNDTILI EMFNKYNSEI LNNIILNLRY KDNNLIDLSG YGAKVEVYDG VELNDKNQFK
LTSSANSKIR VTQNQNIIFN SVFLDFSVSF WIRIPKYKND GIQNYIHNEY TIINCMKNNS
GWKISIRGNR IIWTLIDING KTKSVFFEYN IREDISEYIN RWFFVTITNN LNNAKIYING
KLESNTDIKD IREVIANGEI IFKLDGDIDR TQFIWMKYFS IFNTELSQSN IEERYKIQSY
SEYLKDFWGN PLMYNKEYYM FNAGNKNSYI KLKKDSPVGE ILTRSKYNQN SKYINYRDLY
IGEKFIIRRK SNSQSINDDI VRKEDYIYLD FFNLNQEWRV YTYKYFKKEE EKLFLAPISD
SDEFYNTIQI KEYDEQPTYS CQLLFKKDEE STDEIGLIGI HRFYESGIVF EEYKDYFCIS
KWYLKEVKRK PYNLKLGCNW QFIPKDEGWT E


Related products :

Catalog number Product name Quantity
BP2273 Botulinum neurotoxin type A (light chain) 1 mg
BP2273 Botulinum neurotoxin type A (light chain) 1 mg
BP2273 Botulinum neurotoxin type A (light chain) 1 mg
NB100-73116 Botulinum neurotoxin type A (heavy chain) 0.2 mg
NB100-73116 Botulinum neurotoxin type A (heavy chain) 0.2 mg
3Cb19-24A29 Botulinum neurotoxin type A (heavy chain) 1 mg
3Cb19-24A29 Botulinum neurotoxin type A (heavy chain) 1 mg
610A Botulinum Neurotoxin Type A Light Chain, Recombinant1 10
640A Botulinum Neurotoxin Type F Light Chain, Recombinant1 10
610A Botulinum Neurotoxin Type A Light Chain, Recombinant1 10 µg
630A Botulinum Neurotoxin Type D Light Chain, Recombinant1 10µg
640A Botulinum Neurotoxin Type F Light Chain, Recombinant1 10 µg
620A Botulinum Neurotoxin Type B Light Chain, Recombinant1 10
640B Botulinum Neurotoxin Type F Light Chain, Recombinant1 100
620A Botulinum Neurotoxin Type B Light Chain, Recombinant1 10µg
635A Botulinum Neurotoxin Type E Light Chain, Recombinant1 10
630A Botulinum Neurotoxin Type D Light Chain, Recombinant1 10
625A Botulinum Neurotoxin Type C Light Chain, Recombinant1 10
LST610A Botulinum Neurotoxin Type A Light Chain, recombinant 10 ug.
LST640B Botulinum Neurotoxin Type F Light Chain, recombinant 100 ug.
620A Botulinum Neurotoxin Type B Light Chain, Recombinant1 10 µg
640B Botulinum Neurotoxin Type F Light Chain, Recombinant1 100µg
LST620A Botulinum Neurotoxin Type B Light Chain, recombinant 10 ug.
610A Botulinum Neurotoxin Type A Light Chain, Recombinant1 10µg
LST630A Botulinum Neurotoxin Type D Light Chain, recombinant 10 ug.


 

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