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Basic phospholipase A2 ammodytoxin A (AtxA) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)

 PA2BA_VIPAA             Reviewed;         138 AA.
P00626;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-MAR-1992, sequence version 2.
22-NOV-2017, entry version 114.
RecName: Full=Basic phospholipase A2 ammodytoxin A;
Short=AtxA;
Short=svPLA2;
EC=3.1.1.4;
AltName: Full=Phosphatidylcholine 2-acylhydrolase;
Flags: Precursor;
Vipera ammodytes ammodytes (Western sand viper).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
NCBI_TaxID=8705;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Northern Balkan; TISSUE=Venom gland;
PubMed=2048144; DOI=10.1016/0041-0101(91)90112-5;
Pungercar J., Kordis D., Strukelj B., Liang N.-S., Gubensek F.;
"Cloning and nucleotide sequence of a cDNA encoding ammodytoxin A, the
most toxic phospholipase A2 from the venom of long-nosed viper (Vipera
ammodytes).";
Toxicon 29:269-273(1991).
[2]
PROTEIN SEQUENCE OF 17-138, AND FUNCTION.
STRAIN=Northern Balkan; TISSUE=Venom;
PubMed=3986212; DOI=10.1016/0167-4838(85)90312-7;
Ritonja A., Gubensek F.;
"Ammodytoxin A, a highly lethal phospholipase A2 from Vipera ammodytes
ammodytes venom.";
Biochim. Biophys. Acta 828:306-312(1985).
[3]
MUTAGENESIS OF LYS-114; LYS-117 AND LYS-133, AND LETHAL DOSE.
PubMed=10377255; DOI=10.1042/bj3410139;
Pungercar J., Krizaj I., Liang N.-S., Gubensek F.;
"An aromatic, but not a basic, residue is involved in the toxicity of
group-II phospholipase A2 neurotoxins.";
Biochem. J. 341:139-145(1999).
[4]
CATALYTIC ACTIVITY, AND MUTAGENESIS OF 121-TYR-ILE-122 AND
121-TYR--ASN-125.
PubMed=11027615; DOI=10.1006/bbrc.2000.3605;
Ivanovski G., Copic A., Krizaj I., Gubensek F., Pungercar J.;
"The amino acid region 115-119 of ammodytoxins plays an important role
in neurotoxicity.";
Biochem. Biophys. Res. Commun. 276:1229-1234(2000).
[5]
MUTAGENESIS OF LYS-114; LYS-117 AND 132-LYS--LYS-137.
PubMed=11085916; DOI=10.1042/bj3520251;
Prijatelj P., Copic A., Krizaj I., Gubensek F., Pungercar J.;
"Charge reversal of ammodytoxin A, a phospholipase A2-toxin, does not
abolish its neurotoxicity.";
Biochem. J. 352:251-255(2000).
[6]
FUNCTION.
PubMed=11600150; DOI=10.1016/S0041-0101(01)00170-2;
Fathi B., Rowan E.G., Harvey A.L.;
"The facilitatory actions of snake venom phospholipase A(2)
neurotoxins at the neuromuscular junction are not mediated through
voltage-gated K(+) channels.";
Toxicon 39:1871-1882(2001).
[7]
CATALYTIC ACTIVITY, MUTAGENESIS OF PHE-39, AND LETHAL DOSE.
PubMed=11931665; DOI=10.1042/0264-6021:3630353;
Petan T., Krizaj I., Gubensek F., Pungercar J.;
"Phenylalanine-24 in the N-terminal region of ammodytoxins is
important for both enzymic activity and presynaptic toxicity.";
Biochem. J. 363:353-358(2002).
[8]
AMI2-ATXA CHIMERA.
PubMed=12444963; DOI=10.1046/j.1432-1033.2002.03301.x;
Prijatelj P., Krizaj I., Kralj B., Gubensek F., Pungercar J.;
"The C-terminal region of ammodytoxins is important but not sufficient
for neurotoxicity.";
Eur. J. Biochem. 269:5759-5764(2002).
[9]
CALMODULIN-BINDING, AND MUTAGENESIS OF LYS-114; LYS-117;
121-TYR-ILE-122; 121-TYR--ASN-125 AND 132-LYS--LYS-137.
PubMed=12846835; DOI=10.1046/j.1432-1033.2003.03679.x;
Prijatelj P., Sribar J., Ivanovski G., Krizaj I., Gubensek F.,
Pungercar J.;
"Identification of a novel binding site for calmodulin in ammodytoxin
A, a neurotoxic group IIA phospholipase A2.";
Eur. J. Biochem. 270:3018-3025(2003).
[10]
FUNCTION.
PubMed=15485650; DOI=10.1016/j.bbrc.2004.09.144;
Petrovic U., Sribar J., Paris A., Rupnik M., Krzan M., Vardjan N.,
Gubensek F., Zorec R., Krizaj I.;
"Ammodytoxin, a neurotoxic secreted phospholipase A(2), can act in the
cytosol of the nerve cell.";
Biochem. Biophys. Res. Commun. 324:981-985(2004).
[11]
CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-79; 81-LYS--ARG-84 AND LYS-93,
AND LETHAL DOSE.
PubMed=15488774; DOI=10.1016/j.bbapap.2004.09.002;
Ivanovski G., Petan T., Krizaj I., Gelb M.H., Gubensek F.,
Pungercar J.;
"Basic amino acid residues in the beta-structure region contribute,
but not critically, to presynaptic neurotoxicity of ammodytoxin A.";
Biochim. Biophys. Acta 1702:217-225(2004).
[12]
CATALYTIC ACTIVITY, COFACTOR, SITE, AND MUTAGENESIS OF PHE-39; VAL-46
AND 121-TYR--ASN-125.
TISSUE=Venom;
PubMed=16156665; DOI=10.1021/bi051024r;
Petan T., Krizaj I., Gelb M.H., Pungercar J.;
"Ammodytoxins, potent presynaptic neurotoxins, are also highly
efficient phospholipase A2 enzymes.";
Biochemistry 44:12535-12545(2005).
[13]
FUNCTION, BINDING TO COAGULATION FACTOR X (F10), AND MUTAGENESIS OF
ARG-79; 81-LYS--ARG-84; LYS-114; LYS-117; 121-TYR--ASN-125; LYS-132;
LYS-133 AND 132-LYS--LYS-137.
PubMed=16039772; DOI=10.1016/j.biochi.2005.06.015;
Prijatelj P., Charnay M., Ivanovski G., Jenko Z., Pungercar J.,
Krizaj I., Faure G.;
"The C-terminal and beta-wing regions of ammodytoxin A, a neurotoxic
phospholipase A2 from Vipera ammodytes ammodytes, are critical for
binding to factor Xa and for anticoagulant effect.";
Biochimie 88:69-76(2006).
[14]
FUNCTION, AND BINDING TO M-TYPE PLA2 RECEPTOR (R-180).
PubMed=16815622; DOI=10.1016/j.biochi.2006.06.008;
Prijatelj P., Vardjan N., Rowan E.G., Krizaj I., Pungercar J.;
"Binding to the high-affinity M-type receptor for secreted
phospholipases A(2) is not obligatory for the presynaptic
neurotoxicity of ammodytoxin A.";
Biochimie 88:1425-1433(2006).
[15]
SUBCELLULAR LOCATION.
PubMed=18261469; DOI=10.1016/j.bbamcr.2008.01.011;
Praznikar Z.J., Kovacic L., Rowan E.G., Romih R., Rusmini P.,
Poletti A., Krizaj I., Pungercar J.;
"A presynaptically toxic secreted phospholipase A2 is internalized
into motoneuron-like cells where it is rapidly translocated into the
cytosol.";
Biochim. Biophys. Acta 1783:1129-1139(2008).
[16]
REVIEW.
PubMed=21726572; DOI=10.1016/j.toxicon.2011.06.009;
Krizaj I.;
"Ammodytoxin: a window into understanding presynaptic toxicity of
secreted phospholipases A(2) and more.";
Toxicon 58:219-229(2011).
[17]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 17-138, AND DISULFIDE BONDS.
PubMed=19857576; DOI=10.1016/j.jsb.2009.10.010;
Saul F.A., Prijatelj-Znidarsic P., Vulliez-le Normand B., Villette B.,
Raynal B., Pungercar J., Krizaj I., Faure G.;
"Comparative structural studies of two natural isoforms of
ammodytoxin, phospholipases A2 from Vipera ammodytes ammodytes which
differ in neurotoxicity and anticoagulant activity.";
J. Struct. Biol. 169:360-369(2010).
-!- FUNCTION: Snake venom phospholipase A2 (PLA2) that acts as a
presynaptic neurotoxin, an inhibitor of blood coagulation, and has
been found to bind with high affinity to intracellular proteins.
The response of indirectly stimulated neuromuscular preparations
to ammodytoxin (Atx) is triphasic. The first phase, the transient
inhibition of the acetylcholine (ACh) release, starts soon after
the addition of Atx and lasts for several minutes. This phase is
probably independent of Atx enzymatic activity. The effect may be
due to the specific binding of the toxin to presynaptic receptors.
These receptors, called N-type receptors, are still unidentified.
It is noteworthy that a neuronal isoform of the M-type PLA2
receptor (R180) has been identified as a high-affinity receptor
for Atx in neuronal plasma membranes. It was demonstrated however
that this receptor is not essential for expression of
neurotoxicity by Atx. The second phase corresponds to an
augmentation of neurotransmitter release. A peak is reached 10-20
min after exposure of the preparation to Atx and is followed by a
gradual reduction. In this phase, the enzymatic activity of Atx of
the mammalian is not significant. It is speculated that the
increased release of neurotransmitter in this phase is induced by
the interference of Atx with voltage-gated potassium channels.
Measurements of ionic currents showed however that voltage-gated
potassium channels are not affected by Atx. The third phase of the
response of neuromuscular preparations to Atx, which corresponds
to a complete and irreversible paralysis, is clearly dependent on
the hydrolytic activity of the toxin. In addition to its
presynaptic neurotoxicity, Atx shows an anticoagulant activity by
binding with high affinity to activated coagulation factor X (F10)
thus inhibiting the formation of the prothrombinase complex
(FX/FV) and its activity (IC(50) is 20 nM). Surprisingly, Atx was
discovered to bind intracellular proteins such as calmodulin (CaM)
(IC(50) is 6 nM), 14-3-3 proteins gamma (YWHAG) and epsilon
(YWHAE) (by similarity with AtxC), as well as R25 (by similarity
with AtxC), a mitochondrial integral membrane protein found in
cerebral cortex. These findings raised a doubt about the dogma of
the exclusively extracellular action of PLA2s, defended by the
potential instability of these molecules in the reducing
environment of the eukaryotic cytosol coupled with their possible
inability to act as enzymes in this cellular compartment, due to
too low concentration of calcium ions. This hypothesis was
challenged efficiently by demonstrating the internalization of
AtxA into a culture cells, but still remains to be directly
demonstrated in vivo. PLA2 catalyzes the calcium-dependent
hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
{ECO:0000269|PubMed:11600150, ECO:0000269|PubMed:15485650,
ECO:0000269|PubMed:16039772, ECO:0000269|PubMed:16815622,
ECO:0000269|PubMed:3986212}.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
acylglycerophosphocholine + a carboxylate. {ECO:0000255|PROSITE-
ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036,
ECO:0000269|PubMed:11027615, ECO:0000269|PubMed:11931665,
ECO:0000269|PubMed:15488774, ECO:0000269|PubMed:16156665}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:16156665};
Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:16156665};
-!- SUBUNIT: Monomer. Binds to calmodulin, coagulation factor X (F10),
M-type PLA2 receptor (R-180). May also bind to 14-3-3 proteins
gamma (YWHAG) and epsilon (YWHAE), and R25, a mitochondrial
membrane protein.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18261469}. Host
cytoplasm, host cytosol {ECO:0000269|PubMed:18261469}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- TOXIC DOSE: LD(50) is 0.021 mg/kg by intravenous injection into
mice. {ECO:0000269|PubMed:10377255, ECO:0000269|PubMed:11931665,
ECO:0000269|PubMed:15488774}.
-!- MISCELLANEOUS: Does not affect mKv1.1/KCNA1, rKv1.2/KCNA2,
mKv1.3/KCNA3, hKv1.5/KCNA5 and mKv3.1/KCNC1 voltage-gated
potassium channels. {ECO:0000305|PubMed:11600150}.
-!- SIMILARITY: Belongs to the phospholipase A2 family. Group II
subfamily. D49 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X53471; CAA37567.1; -; mRNA.
PIR; A39561; PSVIAA.
PDB; 3G8G; X-ray; 1.70 A; A=17-138.
PDBsum; 3G8G; -.
ProteinModelPortal; P00626; -.
SMR; P00626; -.
HOVERGEN; HBG008137; -.
EvolutionaryTrace; P00626; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044164; C:host cell cytosol; IEA:UniProtKB-SubCell.
GO; GO:0072556; C:other organism presynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
GO; GO:0102567; F:phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); IEA:UniProtKB-EC.
GO; GO:0102568; F:phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); IEA:UniProtKB-EC.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
CDD; cd00125; PLA2c; 1.
Gene3D; 1.20.90.10; -; 1.
InterPro; IPR001211; PLipase_A2.
InterPro; IPR033112; PLipase_A2_Asp_AS.
InterPro; IPR016090; PLipase_A2_dom.
InterPro; IPR036444; PLipase_A2_dom_sf.
InterPro; IPR033113; PLipase_A2_His_AS.
PANTHER; PTHR11716; PTHR11716; 1.
Pfam; PF00068; Phospholip_A2_1; 1.
PRINTS; PR00389; PHPHLIPASEA2.
SMART; SM00085; PA2c; 1.
SUPFAM; SSF48619; SSF48619; 1.
PROSITE; PS00119; PA2_ASP; 1.
PROSITE; PS00118; PA2_HIS; 1.
1: Evidence at protein level;
3D-structure; Blood coagulation cascade inhibiting toxin; Calcium;
Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
Host cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism;
Metal-binding; Neurotoxin; Presynaptic neurotoxin; Secreted; Signal;
Toxin.
SIGNAL 1 16 {ECO:0000269|PubMed:3986212}.
CHAIN 17 138 Basic phospholipase A2 ammodytoxin A.
/FTId=PRO_0000022970.
ACT_SITE 63 63 {ECO:0000250}.
ACT_SITE 105 105 {ECO:0000250}.
METAL 43 43 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 45 45 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 47 47 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 64 64 Calcium. {ECO:0000250}.
SITE 18 18 Putative membrane binding site.
SITE 19 19 Putative membrane binding site.
SITE 34 34 Putative membrane binding site.
SITE 35 35 Putative membrane binding site.
SITE 39 39 Putative membrane binding site.
SITE 46 46 Putative membrane binding site.
SITE 76 76 Putative membrane binding site.
SITE 77 77 Putative membrane binding site.
SITE 79 79 Putative membrane binding site.
SITE 82 82 Putative membrane binding site.
SITE 124 124 Putative membrane binding site.
SITE 125 125 Putative membrane binding site.
SITE 129 129 Putative membrane binding site.
DISULFID 42 131 {ECO:0000269|PubMed:19857576}.
DISULFID 44 60 {ECO:0000269|PubMed:19857576}.
DISULFID 59 111 {ECO:0000269|PubMed:19857576}.
DISULFID 65 138 {ECO:0000269|PubMed:19857576}.
DISULFID 66 104 {ECO:0000269|PubMed:19857576}.
DISULFID 73 97 {ECO:0000269|PubMed:19857576}.
DISULFID 91 102 {ECO:0000269|PubMed:19857576}.
MUTAGEN 39 39 F->A: Is 4-fold less toxic than wild-type
AtxA, is similarly enzymatically active
on anionic POPG vesicles and 3.2-fold
less active on zwitterionic POPC
vesicles. {ECO:0000269|PubMed:11931665,
ECO:0000269|PubMed:16156665}.
MUTAGEN 39 39 F->N: Is 130-fold less toxic than wild-
type AtxA, is similarly enzymatically
active on anionic POPG vesicles and 3.5-
fold less active on zwitterionic POPC
vesicles. {ECO:0000269|PubMed:11931665,
ECO:0000269|PubMed:16156665}.
MUTAGEN 39 39 F->S: Is 18-fold less toxic than wild-
type AtxA, is similarly enzymatically
active on anionic POPG vesicles and 5.4-
fold less active on zwitterionic POPC
vesicles. {ECO:0000269|PubMed:11931665,
ECO:0000269|PubMed:16156665}.
MUTAGEN 39 39 F->W: Is 8-fold less toxic than wild-type
AtxA, is similarly enzymatically active
on anionic POPG vesicles and on
zwitterionic POPC vesicles.
{ECO:0000269|PubMed:11931665,
ECO:0000269|PubMed:16156665}.
MUTAGEN 39 39 F->Y: Is 16-fold less toxic than wild-
type AtxA, is similarly enzymatically
active on anionic POPG vesicles and on
zwitterionic POPC vesicles.
{ECO:0000269|PubMed:11931665,
ECO:0000269|PubMed:16156665}.
MUTAGEN 46 46 V->W: Is 6-fold less toxic than wild-type
AtxA, has 2-fold higher enzymatic
activity on anionic POPG vesicles and 27-
fold more active on zwitterionic POPC
vesicles. {ECO:0000269|PubMed:16156665}.
MUTAGEN 79 79 R->E: Is 4-fold less toxic than wild-type
AtxA, has 2.5-fold lower enzymatic
activity on anionic POPG vesicles and 6-
fold on zwitterionic POPC vesicles, and
has 8.5-fold lower activity in inhibiting
prothrombinase activity.
{ECO:0000269|PubMed:15488774,
ECO:0000269|PubMed:16039772}.
MUTAGEN 79 79 R->I: Is 1.5-fold less toxic than wild-
type AtxA, and has 1.5-fold higher
enzymatic activity on anionic POPG and
3.5-fold on zwitterionic POPC vesicles.
{ECO:0000269|PubMed:15488774,
ECO:0000269|PubMed:16039772}.
MUTAGEN 79 79 R->K: Is 2.4-fold less toxic than wild-
type AtxA, and has 1.6-fold lower
enzymatic activity on anionic POPG
vesicles and 1.6-fold on zwitterionic
POPC vesicles.
{ECO:0000269|PubMed:15488774,
ECO:0000269|PubMed:16039772}.
MUTAGEN 79 79 R->S: Is 2.6-fold less toxic than wild-
type AtxA, has 1.4-fold lower enzymatic
activity on anionic POPG vesicles and
1.2-fold on zwitterionic POPC vesicles,
and has 3.5-fold lower activity in
inhibiting prothrombinase activity.
{ECO:0000269|PubMed:15488774,
ECO:0000269|PubMed:16039772}.
MUTAGEN 81 84 KYHR->SYSL: Is 13-fold less toxic than
wild-type AtxA, has 1.2-fold lower
enzymatic activity on anionic POPG
vesicles and 1.7-fold on zwitterionic
POPC vesicles, and has 19-fold lower
activity in inhibiting prothrombinase
activity. {ECO:0000269|PubMed:15488774,
ECO:0000269|PubMed:16039772}.
MUTAGEN 93 93 K->A: Is 1.1-fold less toxic than wild-
type AtxA, and has 1.3-fold lower
enzymatic activity on anionic POPG
vesicles and 1.4-fold on zwitterionic
POPC vesicles.
{ECO:0000269|PubMed:15488774}.
MUTAGEN 93 93 K->E: Is 1.5-fold less toxic than wild-
type AtxA, and has 1.1-fold lower
enzymatic activity on anionic POPG
vesicles and 1.2-fold on zwitterionic
POPC vesicles.
{ECO:0000269|PubMed:15488774}.
MUTAGEN 93 93 K->G: Is 1.6-fold less toxic than wild-
type AtxA, and has 1.1-fold lower
enzymatic activity on anionic POPG
vesicles and 1.7-fold on zwitterionic
POPC vesicles.
{ECO:0000269|PubMed:15488774}.
MUTAGEN 93 93 K->R: Is 1.5-fold less toxic than wild-
type AtxA, and is similarly enzymatically
active on anionic POPG vesicles and 1.4-
fold less active on zwitterionic POPC
vesicles. {ECO:0000269|PubMed:15488774}.
MUTAGEN 114 114 K->N: Is 3-fold less toxic (by
intraperitoneal injection) than wild-type
AtxA (by intravenous injection), has 1.6-
fold higher enzymatic activity, has 2.8-
fold lower binding affinity for CaM, and
has similar binding affinity for bovine
brain receptor; when associated with N-
117. {ECO:0000269|PubMed:10377255,
ECO:0000269|PubMed:11085916,
ECO:0000269|PubMed:12846835,
ECO:0000269|PubMed:16039772}.
MUTAGEN 114 114 K->N: Is 30-fold less toxic than wild-
type AtxA, has 3-fold higher enzymatic
activity, has 20-fold lower activity in
inhibiting prothrombinase activity, and
has 4.5-fold lower binding affinity to
CaM; when associated with N-117 and 132-
T--E-137. {ECO:0000269|PubMed:10377255,
ECO:0000269|PubMed:11085916,
ECO:0000269|PubMed:12846835,
ECO:0000269|PubMed:16039772}.
MUTAGEN 117 117 K->N: Is 3-fold less toxic (by
intraperitoneal injection) than wild-type
AtxA (by intravenous injection), has 1.6-
fold higher enzymatic activity, has 2.8-
fold lower binding affinity for CaM, and
has similar binding affinity for bovine
brain receptor; when associated with N-
114. {ECO:0000269|PubMed:10377255,
ECO:0000269|PubMed:11085916,
ECO:0000269|PubMed:12846835,
ECO:0000269|PubMed:16039772}.
MUTAGEN 117 117 K->N: Is 30-fold less toxic than wild-
type AtxA, has 3-fold higher enzymatic
activity, has 20-fold lower activity in
inhibiting prothrombinase activity, and
has 4.5-fold lower binding affinity to
CaM; when associated with N-114 and 132-
T--E-137. {ECO:0000269|PubMed:10377255,
ECO:0000269|PubMed:11085916,
ECO:0000269|PubMed:12846835,
ECO:0000269|PubMed:16039772}.
MUTAGEN 121 125 YIYRN->KKYML: Is >200-fold less toxic
than wild-type AtxA, is similarly
enzymatically active on anionic POPG
vesicles, and 5-fold more active on
zwitterionic POPC vesicles, has 3.5-fold
lower activity in inhibiting
prothrombinase activity, and has 8.3-fold
lower binding affinity for CaM.
{ECO:0000269|PubMed:11027615,
ECO:0000269|PubMed:12846835,
ECO:0000269|PubMed:16039772,
ECO:0000269|PubMed:16156665}.
MUTAGEN 121 122 YI->KK: Is <200-fold less toxic than
wild-type AtxA, has 2-fold lower
enzymatic activity (on
phosphatidylcholine micelle), and has
3.5-fold lower binding affinity for CaM.
{ECO:0000269|PubMed:11027615,
ECO:0000269|PubMed:12846835}.
MUTAGEN 132 137 KKESEK->TETSEE: Is 30-fold less toxic
than wild-type AtxA, has 3-fold higher
enzymatic activity, has 20-fold lower
activity in inhibiting prothrombinase
activity, and has 4.5-fold lower binding
affinity for CaM; when associated with N-
114 and N-117.
{ECO:0000269|PubMed:11085916,
ECO:0000269|PubMed:12846835,
ECO:0000269|PubMed:16039772}.
MUTAGEN 132 132 K->T: Is 2-fold less toxic than wild-type
AtxA, has slight lower enzymatic
activity, has 7-fold lower activity in
inhibiting prothrombinase activity and
has 3.3-fold lower binding affinity to
CaM. {ECO:0000269|PubMed:16039772}.
MUTAGEN 133 133 K->E: Is 2-fold less toxic (by
intraperitoneal injection) than wild-type
AtxA (by intravenous injection), has
similar enzymatic activity, has a
slightly weaker binding affinity for
bovine brain receptor, has 13-fold lower
activity in inhibiting prothrombinase
activity, and has 2.3-fold lower binding
affinity for CaM.
{ECO:0000269|PubMed:10377255,
ECO:0000269|PubMed:16039772}.
HELIX 18 29 {ECO:0000244|PDB:3G8G}.
HELIX 33 36 {ECO:0000244|PDB:3G8G}.
STRAND 37 40 {ECO:0000244|PDB:3G8G}.
TURN 41 43 {ECO:0000244|PDB:3G8G}.
STRAND 44 47 {ECO:0000244|PDB:3G8G}.
HELIX 55 68 {ECO:0000244|PDB:3G8G}.
TURN 75 77 {ECO:0000244|PDB:3G8G}.
STRAND 82 85 {ECO:0000244|PDB:3G8G}.
STRAND 88 91 {ECO:0000244|PDB:3G8G}.
HELIX 96 114 {ECO:0000244|PDB:3G8G}.
HELIX 115 118 {ECO:0000244|PDB:3G8G}.
HELIX 121 123 {ECO:0000244|PDB:3G8G}.
HELIX 128 131 {ECO:0000244|PDB:3G8G}.
SEQUENCE 138 AA; 15531 MW; D9FAF40A04E31BB2 CRC64;
MRTLWIVAVC LIGVEGSLLE FGMMILGETG KNPLTSYSFY GCYCGVGGKG TPKDATDRCC
FVHDCCYGNL PDCSPKTDRY KYHRENGAIV CGKGTSCENR ICECDRAAAI CFRKNLKTYN
YIYRNYPDFL CKKESEKC


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