EzCatDB: D00278
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DB codeD00278
CATH domainDomain 13.10.450.70 : Nuclear Transport Factor 2; Chain
Domain 23.40.30.10 : GlutaredoxinCatalytic domain
E.C.5.3.4.1
CSA1eej

CATH domainRelated DB codes (homologues)
3.40.30.10 : GlutaredoxinS00916,S00279,M00184,D00866,D00869,D00870

Enzyme Name
UniProtKBKEGG

P0AEG6
Protein nameThiol:disulfide interchange protein dsbCprotein disulfide-isomerase
S-S rearrangase
SynonymsNone
RefSeqNP_417369.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_491094.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PfamPF10411 (DsbC_N)
PF13098 (Thioredoxin_2)
[Graphical view]


UniProtKB:Accession NumberP0AEG6
Entry nameDSBC_ECOLI
Activity
SubunitHomodimer.
Subcellular locationPeriplasm.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC02582C02582
CompoundProtein disulfideProtein disulfide
Typedisulfide bond,peptide/proteindisulfide bond,peptide/protein
ChEBI

PubChem

          
1eejA01UnboundUnbound
1eejB01UnboundUnbound
1g0tA01UnboundUnbound
1g0tB01UnboundUnbound
1jzdA01UnboundUnbound
1jzdB01UnboundUnbound
1jzoA01UnboundUnbound
1jzoB01UnboundUnbound
1tjdA01UnboundUnbound
1eejA02UnboundUnbound
1eejB02UnboundUnbound
1g0tA02UnboundUnbound
1g0tB02UnboundUnbound
1jzdA02UnboundUnbound
1jzdB02UnboundUnbound
1jzoA02UnboundUnbound
1jzoB02UnboundUnbound
1tjdA02UnboundUnbound

Active-site residues
resource
literature [3], [4]
pdbCatalytic residuescomment
          
1eejA01              
 
1eejB01              
 
1g0tA01              
 
1g0tB01              
 
1jzdA01              
 
1jzdB01              
 
1jzoA01              
 
1jzoB01              
 
1tjdA01              
 
1eejA02CYS 98;CYS 101
 
1eejB02CYS 98;CYS 101
 
1g0tA02CYS 98;       
mutant C101S
1g0tB02CYS 98;       
mutant C101S
1jzdA02CYS 98;       
mutant C101S
1jzdB02CYS 98;       
mutant C101S
1jzoA02CYS 98;       
mutant C101S
1jzoB02CYS 98;       
mutant C101S
1tjdA02CYS 98;CYS 101
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]Fig.8, p.15815
[4]p.197-198
[7]p.4780-4781
[8]p.120-121
[9]

[11]Fig.1

references
[1]
CommentsCHARACTERIZATION.
Medline ID94222048
PubMed ID8168497
JournalEMBO J
Year1994
Volume13
Pages2007-12
AuthorsShevchik VE, Condemine G, Robert-Baudouy J
TitleCharacterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity.
Related UniProtKBP21892
[2]
CommentsCHARACTERIZATION, MUTAGENESIS, AND REVISION TO 219.
Medline ID95226395
PubMed ID7536035
JournalBiochemistry
Year1995
Volume34
Pages5075-89
AuthorsZapun A, Missiakas D, Raina S, Creighton TE
TitleStructural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli.
Related UniProtKBP21892
[3]
PubMed ID9398311
JournalBiochemistry
Year1997
Volume36
Pages15810-6
AuthorsChivers PT, Raines RT
TitleGeneral acid/base catalysis in the active site of Escherichia coli thioredoxin.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID20165176
PubMed ID10700276
JournalNat Struct Biol
Year2000
Volume7
Pages196-9
AuthorsMcCarthy AA, Haebel PW, Torronen A, Rybin V, Baker EN, Metcalf P
TitleCrystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli.
Related PDB1eej
Related UniProtKBP21892
[5]
PubMed ID11886218
JournalJ Struct Biol
Year2001
Volume136
Pages162-6
AuthorsHaebel PW, Wichman S, Goldstone D, Metcalf P
TitleCrystallization and initial crystallographic analysis of the disulfide bond isomerase DsbC in complex with the alpha domain of the electron transporter DsbD.
[6]
PubMed ID11493705
JournalProc Natl Acad Sci U S A
Year2001
Volume98
Pages9551-6
AuthorsGoldstone D, Haebel PW, Katzen F, Bader MW, Bardwell JC, Beckwith J, Metcalf P
TitleDsbC activation by the N-terminal domain of DsbD.
[7]
PubMed ID12234918
JournalEMBO J
Year2002
Volume21
Pages4774-84
AuthorsHaebel PW, Goldstone D, Katzen F, Beckwith J, Metcalf P
TitleThe disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.
Related PDB1g0t,1jzo,1jzd
[8]
PubMed ID12524212
JournalAnnu Rev Biochem
Year2003
Volume72
Pages111-35
AuthorsKadokura H, Katzen F, Beckwith J
TitleProtein disulfide bond formation in prokaryotes.
[9]
PubMed ID15388920
JournalActa Crystallogr D Biol Crystallogr
Year2004
Volume60
Pages1747-52
AuthorsBanaszak K, Mechin I, Frost G, Rypniewski W
TitleStructure of the reduced disulfide-bond isomerase DsbC from Escherichia coli.
Related PDB1tjd
[10]
PubMed ID15057279
JournalEMBO J
Year2004
Volume23
Pages1709-19
AuthorsRozhkova A, Stirnimann CU, Frei P, Grauschopf U, Brunisholz R, Grutter MG, Capitani G, Glockshuber R
TitleStructural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD.
[11]
PubMed ID15546661
JournalBiochim Biophys Acta
Year2004
Volume1694
Pages111-9
AuthorsNakamoto H, Bardwell JC
TitleCatalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm.

comments
According to the literature [11], this enzyme catalyzes the following reaction.
(A) Electron transfer from the active site (Cys98/Cys101) to the disulfide bond of the misfolded substrate protein, producing correctly folded protein.
(B) Electron transfer from DsbD enzyme (Swissprot;P36655) to the disulfide bond of the active site, recovering the active site.

createdupdated
2005-06-142009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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