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Bifunctional glutathionylspermidine synthetase/amidase (GspSA) [Includes: Glutathionylspermidine amidase (Gsp amidase) (EC 3.5.1.78) (Glutathionylspermidine amidohydrolase [spermidine-forming]); Glutathionylspermidine synthetase (Gsp synthetase) (EC 6.3.1.8) (Glutathione:spermidine ligase [ADP-forming]) (Gsp synthase)]

 GSP_ECOLI               Reviewed;         619 AA.
P0AES0; P43675; Q2M9K7;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 1.
28-MAR-2018, entry version 100.
RecName: Full=Bifunctional glutathionylspermidine synthetase/amidase;
Short=GspSA;
Includes:
RecName: Full=Glutathionylspermidine amidase;
Short=Gsp amidase;
EC=3.5.1.78 {ECO:0000269|PubMed:20530482, ECO:0000269|PubMed:23097746, ECO:0000269|PubMed:7775463, ECO:0000269|PubMed:8999955};
AltName: Full=Glutathionylspermidine amidohydrolase [spermidine-forming];
Includes:
RecName: Full=Glutathionylspermidine synthetase;
Short=Gsp synthetase;
EC=6.3.1.8 {ECO:0000269|PubMed:20530482, ECO:0000269|PubMed:23097746, ECO:0000269|PubMed:7775463, ECO:0000269|PubMed:8999955};
AltName: Full=Glutathione:spermidine ligase [ADP-forming];
AltName: Full=Gsp synthase;
Name=gss; Synonyms=gsp; OrderedLocusNames=b2988, JW2956;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-7, FUNCTION,
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
STRAIN=B, and K12;
PubMed=7775463; DOI=10.1074/jbc.270.23.14031;
Bollinger J.M. Jr., Kwon D.S., Huisman G.W., Kolter R., Walsh C.T.;
"Glutathionylspermidine metabolism in Escherichia coli. Purification,
cloning, overproduction, and characterization of a bifunctional
glutathionylspermidine synthetase/amidase.";
J. Biol. Chem. 270:14031-14041(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
REACTION MECHANISM OF AMIDASE ACTIVITY, ACTIVE SITE AT CYS-59, ENZYME
REGULATION, AND MUTAGENESIS OF CYS-59 AND CYS-173.
PubMed=9398217; DOI=10.1021/bi9714464;
Lin C.H., Kwon D.S., Bollinger J.M. Jr., Walsh C.T.;
"Evidence for a glutathionyl-enzyme intermediate in the amidase
activity of the bifunctional glutathionylspermidine synthetase/amidase
from Escherichia coli.";
Biochemistry 36:14930-14938(1997).
[5]
FUNCTION, CATALYTIC ACTIVITY, DOMAIN, SUBSTRATE SPECIFICITY, AND
ENZYME REGULATION.
PubMed=8999955; DOI=10.1074/jbc.272.4.2429;
Kwon D.S., Lin C.H., Chen S., Coward J.K., Walsh C.T.,
Bollinger J.M. Jr.;
"Dissection of glutathionylspermidine synthetase/amidase from
Escherichia coli into autonomously folding and functional synthetase
and amidase domains.";
J. Biol. Chem. 272:2429-2436(1997).
[6]
FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
STRAIN=K12;
PubMed=23097746;
Sui L., Warren J.C., Russell J.P., Stourman N.V.;
"Comparison of the functions of glutathionylspermidine
synthetase/amidase from E. coli and its predicted homologues YgiC and
YjfC.";
Int. J. Biochem. Mol. Biol. 3:302-312(2012).
[7]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME AND IN COMPLEXES
WITH SUBSTRATE; PRODUCT AND INHIBITOR, DOMAIN BOUNDARIES, SUBUNIT,
REACTION MECHANISM OF SYNTHETASE ACTIVITY, KINETIC PARAMETERS, SITE AT
ARG-316, AND MUTAGENESIS OF SER-335; SER-337; CYS-338; GLU-391;
GLU-392; THR-441; ARG-538 AND ARG-598.
PubMed=17124497; DOI=10.1038/sj.emboj.7601440;
Pai C.H., Chiang B.Y., Ko T.P., Chou C.C., Chong C.M., Yen F.J.,
Chen S., Coward J.K., Wang A.H., Lin C.H.;
"Dual binding sites for translocation catalysis by Escherichia coli
glutathionylspermidine synthetase.";
EMBO J. 25:5970-5982(2006).
[8]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1-197, FUNCTION, ROLE IN
REDOX REGULATION, CATALYTIC ACTIVITY, ENZYME REGULATION, OXIDATION AT
CYS-59, AND DISRUPTION PHENOTYPE.
PubMed=20530482; DOI=10.1074/jbc.M110.133363;
Chiang B.Y., Chen T.C., Pai C.H., Chou C.C., Chen H.H., Ko T.P.,
Hsu W.H., Chang C.Y., Wu W.F., Wang A.H., Lin C.H.;
"Protein S-thiolation by glutathionylspermidine (Gsp): the role of
Escherichia coli Gsp synthetase/amidase in redox regulation.";
J. Biol. Chem. 285:25345-25353(2010).
[9]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF MUTANT ALA-59 IN COMPLEXES
WITH ADP; GLUTATHIONYLSPERMIDINE AND MAGNESIUM, ACTIVE SITES, AND
CATALYTIC MECHANISM OF AMIDASE ACTIVITY.
PubMed=21226054; DOI=10.1002/pro.589;
Pai C.H., Wu H.J., Lin C.H., Wang A.H.;
"Structure and mechanism of Escherichia coli glutathionylspermidine
amidase belonging to the family of cysteine; histidine-dependent
amidohydrolases/peptidases.";
Protein Sci. 20:557-566(2011).
-!- FUNCTION: Catalyzes the formation of an amide bond between
glutathione (GSH) and spermidine coupled with hydrolysis of ATP;
also catalyzes the opposing reaction, i.e. the hydrolysis of
glutathionylspermidine (Gsp) back to glutathione and spermidine.
The amidase active site can also hydrolyze Gsp-disulfide (Gsp-S-S-
Gsp) to Gsp-SG and Gsp S-thiolated proteins (GspSSPs) to GSH S-
thiolated protein (GSSPs). Likely acts synergistically with
glutaredoxin to regulate the redox environment of E.coli and
defend against oxidative damage. In vitro, the amidase active site
also catalyzes hydrolysis of amide and ester derivatives of
glutathione (e.g. glutathione ethyl ester and glutathione amide)
but lacks activity toward acetylspermidine (N1 and N8) and
acetylspermine (N1). {ECO:0000269|PubMed:20530482,
ECO:0000269|PubMed:23097746, ECO:0000269|PubMed:7775463,
ECO:0000269|PubMed:8999955}.
-!- CATALYTIC ACTIVITY: Glutathione + spermidine + ATP =
glutathionylspermidine + ADP + phosphate.
{ECO:0000269|PubMed:20530482, ECO:0000269|PubMed:23097746,
ECO:0000269|PubMed:7775463, ECO:0000269|PubMed:8999955}.
-!- CATALYTIC ACTIVITY: Glutathionylspermidine + H(2)O = glutathione +
spermidine. {ECO:0000269|PubMed:20530482,
ECO:0000269|PubMed:23097746, ECO:0000269|PubMed:7775463,
ECO:0000269|PubMed:8999955}.
-!- ENZYME REGULATION: When exposed to oxidative stress, Gsp amidase
activity is transiently inhibited in vivo by oxidation of the
catalytic Cys-59 thiol to sulfenic acid; this modification does
not affect Gsp synthetase activity. Gsp amidase activity is
negatively autoregulated by the Gsp synthetase domain, and is
activated by the Gsp synthetase substrates, GSH and ATP-Mg(2+);
the occupancy of the synthetase active site may initiate
communication through the protein as manifest by the release of
inhibition of the amidase activity. A tetrahedral phosphonate
analog of glutathionylspermidine, designed as a mimic of the
proposed tetrahedral intermediate for either reaction, inhibits
the synthetase activity (Ki of 10 uM) but does not inhibit the
amidase activity. Amidase activity is inhibited by iodoacetamide
in vitro. {ECO:0000269|PubMed:20530482,
ECO:0000269|PubMed:8999955, ECO:0000269|PubMed:9398217}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=100 uM for ATP (at pH 6.8) {ECO:0000269|PubMed:17124497,
ECO:0000269|PubMed:7775463};
KM=800 uM for glutathione (at pH 6.8)
{ECO:0000269|PubMed:17124497, ECO:0000269|PubMed:7775463};
KM=218 uM for glutathione {ECO:0000269|PubMed:17124497,
ECO:0000269|PubMed:7775463};
KM=60 uM for spermidine (at pH 6.8)
{ECO:0000269|PubMed:17124497, ECO:0000269|PubMed:7775463};
KM=20 uM for spermidine (at pH 7.5)
{ECO:0000269|PubMed:17124497, ECO:0000269|PubMed:7775463};
KM=76 uM for spermidine {ECO:0000269|PubMed:17124497,
ECO:0000269|PubMed:7775463};
KM=900 uM for glutathionylspermidine (at pH 7.5)
{ECO:0000269|PubMed:17124497, ECO:0000269|PubMed:7775463};
Note=kcat is 7 sec(-1) for Gsp synthetase activity at pH 6.8 and
2.1 sec(-1) for Gsp amidase activity at pH 7.5.
{ECO:0000269|PubMed:7775463};
pH dependence:
Optimum pH is around 6.8 for Gsp synthetase activity.
{ECO:0000269|PubMed:7775463};
-!- PATHWAY: Sulfur metabolism; glutathione metabolism.
-!- PATHWAY: Amine and polyamine metabolism; spermidine metabolism.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17124497,
ECO:0000269|PubMed:7775463}.
-!- INTERACTION:
P31574:fixB; NbExp=2; IntAct=EBI-557080, EBI-554030;
P0AG30:rho; NbExp=5; IntAct=EBI-557080, EBI-545468;
-!- INDUCTION: Expression level is unaffected by H(2)O(2); however Gsp
rapidly accumulates in E.coli in the presence of H(2)O(2).
-!- DOMAIN: The two activities reside in distinct domains (N-terminal
amidase and C-terminal synthetase). The two domains expressed
independently are folded and functional; liberation of the amidase
domain from the synthetase domain highly activates the amidase
activity. {ECO:0000269|PubMed:17124497,
ECO:0000269|PubMed:8999955}.
-!- PTM: Oxidation of Cys-59 to sulfenic acid during oxidative stress
selectively inhibits the amidase activity which leads to a rapid
increase in the amounts of intracellular Gsp and Gsp S-thiolated
proteins (GspSSPs). {ECO:0000269|PubMed:20530482}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene do not produce Gsp
under anaerobic conditions. Cells lacking both this gene and
glutaredoxin (grxA or grxB) become hypersensitive to H(2)O(2);
they are even more susceptible to oxidative damage than the single
mutant lacking glutaredoxin only. {ECO:0000269|PubMed:20530482,
ECO:0000269|PubMed:23097746}.
-!- MISCELLANEOUS: Gsp forms mixed disulfides with the thiols of a
variety of E.coli proteins. These mixed disulfides represent a
previously uncharacterized type of post-translational
modification. The level of these proteins is increased by
oxidative stress, which implies that Gsp might protect protein
thiols against irreversible oxidation (PubMed:20530482).
{ECO:0000305|PubMed:20530482}.
-!- MISCELLANEOUS: No metal ion is required for the amidase activity.
{ECO:0000305|PubMed:8999955}.
-!- MISCELLANEOUS: Gsp hydrolysis to GSH and spermidine proceeds with
formation of a glutathionyl acyl-enzyme intermediate, utilizing a
cysteine residue as the catalytic nucleophile (PubMed:9398217).
For Gsp synthesis, GSH is likely phosphorylated at one of two GSH-
binding sites to form an acylphosphate intermediate that then
translocates to the other site for subsequent nucleophilic
addition of spermidine (PubMed:17124497).
{ECO:0000305|PubMed:17124497, ECO:0000305|PubMed:9398217}.
-!- SIMILARITY: In the C-terminal section; belongs to the
glutathionylspermidine synthase preATP-grasp family.
{ECO:0000305}.
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EMBL; U23148; AAC43339.1; -; Genomic_DNA.
EMBL; U28377; AAA69155.1; -; Genomic_DNA.
EMBL; U00096; AAC76024.1; -; Genomic_DNA.
EMBL; AP009048; BAE77049.1; -; Genomic_DNA.
PIR; A57538; A57538.
RefSeq; NP_417462.1; NC_000913.3.
RefSeq; WP_001297309.1; NZ_LN832404.1.
PDB; 2IO7; X-ray; 2.70 A; A/B=1-619.
PDB; 2IO8; X-ray; 2.10 A; A/B=1-619.
PDB; 2IO9; X-ray; 2.20 A; A/B=1-619.
PDB; 2IOA; X-ray; 2.80 A; A/B=1-619.
PDB; 2IOB; X-ray; 2.20 A; A/B=1-619.
PDB; 3A2Y; X-ray; 1.95 A; A=1-197.
PDB; 3A2Z; X-ray; 1.50 A; A=1-197.
PDB; 3A30; X-ray; 2.20 A; A=1-197.
PDB; 3O98; X-ray; 2.80 A; A/B=1-619.
PDBsum; 2IO7; -.
PDBsum; 2IO8; -.
PDBsum; 2IO9; -.
PDBsum; 2IOA; -.
PDBsum; 2IOB; -.
PDBsum; 3A2Y; -.
PDBsum; 3A2Z; -.
PDBsum; 3A30; -.
PDBsum; 3O98; -.
ProteinModelPortal; P0AES0; -.
SMR; P0AES0; -.
BioGrid; 4261180; 18.
DIP; DIP-36018N; -.
IntAct; P0AES0; 14.
STRING; 316385.ECDH10B_3165; -.
MEROPS; C51.A01; -.
PaxDb; P0AES0; -.
PRIDE; P0AES0; -.
EnsemblBacteria; AAC76024; AAC76024; b2988.
EnsemblBacteria; BAE77049; BAE77049; BAE77049.
GeneID; 947474; -.
KEGG; ecj:JW2956; -.
KEGG; eco:b2988; -.
PATRIC; fig|1411691.4.peg.3741; -.
EchoBASE; EB2720; -.
EcoGene; EG12882; gss.
eggNOG; ENOG4106032; Bacteria.
eggNOG; COG0754; LUCA.
HOGENOM; HOG000124980; -.
InParanoid; P0AES0; -.
KO; K01460; -.
OMA; YMGYKWQ; -.
BioCyc; EcoCyc:GSP-MONOMER; -.
BioCyc; MetaCyc:GSP-MONOMER; -.
BRENDA; 3.5.1.78; 2026.
BRENDA; 6.3.1.8; 2026.
UniPathway; UPA00204; -.
UniPathway; UPA00819; -.
EvolutionaryTrace; P0AES0; -.
PRO; PR:P0AES0; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008884; F:glutathionylspermidine amidase activity; IDA:EcoCyc.
GO; GO:0008885; F:glutathionylspermidine synthase activity; IDA:EcoCyc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006749; P:glutathione metabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0008216; P:spermidine metabolic process; IEA:UniProtKB-UniPathway.
InterPro; IPR007921; CHAP_dom.
InterPro; IPR005494; GSPS_pre-ATP-grasp-like_dom.
InterPro; IPR016185; PreATP-grasp_dom_sf.
Pfam; PF05257; CHAP; 1.
Pfam; PF03738; GSP_synth; 1.
SUPFAM; SSF52440; SSF52440; 1.
PROSITE; PS50911; CHAP; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome;
Direct protein sequencing; Hydrolase; Ligase; Magnesium;
Metal-binding; Multifunctional enzyme; Nucleotide-binding; Oxidation;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7775463}.
CHAIN 2 619 Bifunctional glutathionylspermidine
synthetase/amidase.
/FTId=PRO_0000070443.
DOMAIN 34 176 Peptidase C51. {ECO:0000255|PROSITE-
ProRule:PRU00048}.
NP_BIND 316 318 ATP.
NP_BIND 539 540 ATP.
NP_BIND 568 571 ATP.
NP_BIND 603 605 ATP.
REGION 2 195 Gsp amidase.
REGION 78 81 Gsp binding.
REGION 196 205 Linker.
REGION 206 619 Gsp synthetase.
ACT_SITE 59 59 S-(gamma-glutamyl-cysteinyl-glycyl)-
cysteine intermediate.
{ECO:0000269|PubMed:9398217}.
METAL 318 318 Magnesium 1.
METAL 330 330 Magnesium 1.
METAL 330 330 Magnesium 2.
METAL 332 332 Magnesium 2.
BINDING 58 58 Gsp.
BINDING 64 64 Gsp.
BINDING 149 149 Gsp.
BINDING 316 316 Glutathione.
BINDING 335 335 Glutathione.
BINDING 391 391 Spermidine.
BINDING 392 392 Glutathione.
BINDING 446 446 Glutathione.
BINDING 498 498 ATP.
BINDING 533 533 ATP.
BINDING 582 582 ATP.
BINDING 610 610 Spermidine.
SITE 131 131 Increases nucleophilicity of active site
Cys; for amidase activity.
SITE 316 316 Transition state stabilizer; for
synthetase activity.
MOD_RES 59 59 Cysteine sulfenic acid (-SOH); transient.
{ECO:0000269|PubMed:20530482}.
MUTAGEN 59 59 C->A: Loss of amidase activity.
{ECO:0000269|PubMed:9398217}.
MUTAGEN 173 173 C->A: No effect on amidase activity.
{ECO:0000269|PubMed:9398217}.
MUTAGEN 316 316 R->E: Loss of synthetase activity.
MUTAGEN 335 335 S->A: 3.6-fold decrease in GSH affinity,
1.6-fold decrease in spermidine activity,
and 1.3-fold decrease in synthetase
activity. {ECO:0000269|PubMed:17124497}.
MUTAGEN 337 337 S->A: No effect on GSH and spermidine
affinity, but 2-fold decrease in
synthetase activity.
{ECO:0000269|PubMed:17124497}.
MUTAGEN 338 338 C->A: 10-fold decrease in GSH affinity,
5-fold decrease in spermidine activity,
but no effect on synthetase activity.
{ECO:0000269|PubMed:17124497}.
MUTAGEN 391 391 E->A: 2-fold decrease in GSH affinity,
60-fold decrease in spermidine activity,
and 10-fold decrease in synthetase
activity. {ECO:0000269|PubMed:17124497}.
MUTAGEN 392 392 E->A: 33-fold decrease in GSH affinity,
13-fold decrease in spermidine activity,
and 6-fold decrease in synthetase
activity. {ECO:0000269|PubMed:17124497}.
MUTAGEN 441 441 T->A: 3-fold decrease in GSH affinity,
21-fold decrease in spermidine activity,
and 17-fold decrease in synthetase
activity. {ECO:0000269|PubMed:17124497}.
MUTAGEN 538 538 R->A: 6-fold decrease in GSH affinity,
2.4-fold decrease in spermidine activity,
and 4-fold decrease in synthetase
activity. {ECO:0000269|PubMed:17124497}.
MUTAGEN 598 598 R->A: 10-fold increase in GSH affinity,
9-fold decrease in spermidine activity,
and 15-fold decrease in synthetase
activity. {ECO:0000269|PubMed:17124497}.
STRAND 15 19 {ECO:0000244|PDB:3A2Z}.
TURN 20 22 {ECO:0000244|PDB:3A2Z}.
STRAND 23 26 {ECO:0000244|PDB:3A2Z}.
HELIX 35 40 {ECO:0000244|PDB:3A2Z}.
HELIX 42 44 {ECO:0000244|PDB:3A2Z}.
STRAND 45 48 {ECO:0000244|PDB:3A2Z}.
STRAND 51 55 {ECO:0000244|PDB:3A2Z}.
HELIX 59 71 {ECO:0000244|PDB:3A2Z}.
STRAND 72 74 {ECO:0000244|PDB:3A2Z}.
HELIX 81 86 {ECO:0000244|PDB:3A2Z}.
STRAND 89 92 {ECO:0000244|PDB:3A2Z}.
TURN 93 95 {ECO:0000244|PDB:3A2Z}.
STRAND 98 100 {ECO:0000244|PDB:3A2Z}.
STRAND 102 105 {ECO:0000244|PDB:3A2Z}.
STRAND 108 110 {ECO:0000244|PDB:2IOB}.
STRAND 117 120 {ECO:0000244|PDB:3A2Z}.
HELIX 124 126 {ECO:0000244|PDB:3A2Z}.
TURN 127 129 {ECO:0000244|PDB:3A2Z}.
STRAND 131 138 {ECO:0000244|PDB:3A2Z}.
STRAND 140 146 {ECO:0000244|PDB:3A2Z}.
STRAND 148 150 {ECO:0000244|PDB:3A2Z}.
STRAND 162 170 {ECO:0000244|PDB:3A2Z}.
STRAND 173 177 {ECO:0000244|PDB:3A2Z}.
STRAND 179 182 {ECO:0000244|PDB:3A2Z}.
STRAND 185 192 {ECO:0000244|PDB:3A2Z}.
HELIX 206 209 {ECO:0000244|PDB:2IO8}.
STRAND 212 215 {ECO:0000244|PDB:2IO8}.
STRAND 229 231 {ECO:0000244|PDB:2IOA}.
HELIX 232 241 {ECO:0000244|PDB:2IO8}.
STRAND 245 247 {ECO:0000244|PDB:2IO8}.
STRAND 251 256 {ECO:0000244|PDB:2IO8}.
HELIX 257 283 {ECO:0000244|PDB:2IO8}.
HELIX 285 288 {ECO:0000244|PDB:2IO8}.
HELIX 289 291 {ECO:0000244|PDB:2IO8}.
HELIX 295 297 {ECO:0000244|PDB:2IO8}.
HELIX 298 307 {ECO:0000244|PDB:2IO8}.
HELIX 309 311 {ECO:0000244|PDB:2IOB}.
STRAND 314 322 {ECO:0000244|PDB:2IO8}.
STRAND 325 332 {ECO:0000244|PDB:2IO8}.
HELIX 339 343 {ECO:0000244|PDB:2IO8}.
HELIX 345 353 {ECO:0000244|PDB:2IO8}.
TURN 361 364 {ECO:0000244|PDB:2IO8}.
HELIX 365 374 {ECO:0000244|PDB:2IO8}.
STRAND 380 386 {ECO:0000244|PDB:2IO8}.
HELIX 390 405 {ECO:0000244|PDB:2IO8}.
STRAND 409 416 {ECO:0000244|PDB:2IO8}.
STRAND 423 425 {ECO:0000244|PDB:2IO8}.
STRAND 437 442 {ECO:0000244|PDB:2IO8}.
HELIX 444 453 {ECO:0000244|PDB:2IO8}.
TURN 456 458 {ECO:0000244|PDB:2IOB}.
STRAND 459 461 {ECO:0000244|PDB:2IOB}.
HELIX 475 479 {ECO:0000244|PDB:2IO8}.
STRAND 485 488 {ECO:0000244|PDB:2IO8}.
HELIX 490 493 {ECO:0000244|PDB:2IO8}.
TURN 494 496 {ECO:0000244|PDB:2IO8}.
HELIX 500 507 {ECO:0000244|PDB:2IO8}.
STRAND 517 520 {ECO:0000244|PDB:2IO8}.
HELIX 523 528 {ECO:0000244|PDB:2IO8}.
STRAND 530 534 {ECO:0000244|PDB:2IO8}.
TURN 539 542 {ECO:0000244|PDB:2IO8}.
STRAND 544 546 {ECO:0000244|PDB:2IO8}.
STRAND 552 555 {ECO:0000244|PDB:2IO8}.
TURN 559 562 {ECO:0000244|PDB:2IO8}.
STRAND 565 569 {ECO:0000244|PDB:2IO8}.
STRAND 579 588 {ECO:0000244|PDB:2IO8}.
STRAND 591 604 {ECO:0000244|PDB:2IO8}.
STRAND 609 612 {ECO:0000244|PDB:2IO8}.
STRAND 614 617 {ECO:0000244|PDB:2IO8}.
SEQUENCE 619 AA; 70532 MW; 07FB43D8A0B2933C CRC64;
MSKGTTSQDA PFGTLLGYAP GGVAIYSSDY SSLDPQEYED DAVFRSYIDD EYMGHKWQCV
EFARRFLFLN YGVVFTDVGM AWEIFSLRFL REVVNDNILP LQAFPNGSPR APVAGALLIW
DKGGEFKDTG HVAIITQLHG NKVRIAEQNV IHSPLPQGQQ WTRELEMVVE NGCYTLKDTF
DDTTILGWMI QTEDTEYSLP QPEIAGELLK ISGARLENKG QFDGKWLDEK DPLQNAYVQA
NGQVINQDPY HYYTITESAE QELIKATNEL HLMYLHATDK VLKDDNLLAL FDIPKILWPR
LRLSWQRRRH HMITGRMDFC MDERGLKVYE YNADSASCHT EAGLILERWA EQGYKGNGFN
PAEGLINELA GAWKHSRARP FVHIMQDKDI EENYHAQFME QALHQAGFET RILRGLDELG
WDAAGQLIDG EGRLVNCVWK TWAWETAFDQ IREVSDREFA AVPIRTGHPQ NEVRLIDVLL
RPEVLVFEPL WTVIPGNKAI LPILWSLFPH HRYLLDTDFT VNDELVKTGY AVKPIAGRCG
SNIDLVSHHE EVLDKTSGKF AEQKNIYQQL WCLPKVDGKY IQVCTFTVGG NYGGTCLRGD
ESLVIKKESD IEPLIVVKK


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