DB code: D00278

CATH domain 3.10.450.70 : Nuclear Transport Factor 2; Chain
3.40.30.10 : Glutaredoxin Catalytic domain
E.C. 5.3.4.1
CSA 1eej
M-CSA 1eej
MACiE

CATH domain Related DB codes (homologues)
3.40.30.10 : Glutaredoxin S00916 S00279 M00184 D00866 D00869 D00870

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P0AEG6 Thiol:disulfide interchange protein dsbC
None NP_417369.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_491094.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF10411 (DsbC_N)
PF13098 (Thioredoxin_2)
[Graphical View]

KEGG enzyme name
protein disulfide-isomerase
S-S rearrangase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P0AEG6 DSBC_ECOLI Homodimer. Periplasm.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C02582 C02582
E.C.
Compound Protein disulfide Protein disulfide
Type disulfide bond,peptide/protein disulfide bond,peptide/protein
ChEBI
PubChem
1eejA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1eejB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1g0tA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1g0tB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1jzdA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1jzdB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1jzoA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1jzoB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1tjdA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1eejA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1eejB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1g0tA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1g0tB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1jzdA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1jzdB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1jzoA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1jzoB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1tjdA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [3], [4]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1eejA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1eejB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1g0tA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1g0tB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jzdA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jzdB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jzoA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jzoB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1tjdA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1eejA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 98;CYS 101
1eejB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 98;CYS 101
1g0tA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 98; mutant C101S
1g0tB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 98; mutant C101S
1jzdA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 98; mutant C101S
1jzdB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 98; mutant C101S
1jzoA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 98; mutant C101S
1jzoB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 98; mutant C101S
1tjdA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 98;CYS 101

References for Catalytic Mechanism
References Sections No. 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]
Resource
Comments CHARACTERIZATION.
Medline ID 94222048
PubMed ID 8168497
Journal EMBO J
Year 1994
Volume 13
Pages 2007-12
Authors Shevchik VE, Condemine G, Robert-Baudouy J
Title Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity.
Related PDB
Related UniProtKB P21892
[2]
Resource
Comments CHARACTERIZATION, MUTAGENESIS, AND REVISION TO 219.
Medline ID 95226395
PubMed ID 7536035
Journal Biochemistry
Year 1995
Volume 34
Pages 5075-89
Authors Zapun A, Missiakas D, Raina S, Creighton TE
Title Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli.
Related PDB
Related UniProtKB P21892
[3]
Resource
Comments
Medline ID
PubMed ID 9398311
Journal Biochemistry
Year 1997
Volume 36
Pages 15810-6
Authors Chivers PT, Raines RT
Title General acid/base catalysis in the active site of Escherichia coli thioredoxin.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID 20165176
PubMed ID 10700276
Journal Nat Struct Biol
Year 2000
Volume 7
Pages 196-9
Authors McCarthy AA, Haebel PW, Torronen A, Rybin V, Baker EN, Metcalf P
Title Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli.
Related PDB 1eej
Related UniProtKB P21892
[5]
Resource
Comments
Medline ID
PubMed ID 11886218
Journal J Struct Biol
Year 2001
Volume 136
Pages 162-6
Authors Haebel PW, Wichman S, Goldstone D, Metcalf P
Title Crystallization and initial crystallographic analysis of the disulfide bond isomerase DsbC in complex with the alpha domain of the electron transporter DsbD.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 11493705
Journal Proc Natl Acad Sci U S A
Year 2001
Volume 98
Pages 9551-6
Authors Goldstone D, Haebel PW, Katzen F, Bader MW, Bardwell JC, Beckwith J, Metcalf P
Title DsbC activation by the N-terminal domain of DsbD.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 12234918
Journal EMBO J
Year 2002
Volume 21
Pages 4774-84
Authors Haebel PW, Goldstone D, Katzen F, Beckwith J, Metcalf P
Title The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.
Related PDB 1g0t 1jzo 1jzd
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 12524212
Journal Annu Rev Biochem
Year 2003
Volume 72
Pages 111-35
Authors Kadokura H, Katzen F, Beckwith J
Title Protein disulfide bond formation in prokaryotes.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 15388920
Journal Acta Crystallogr D Biol Crystallogr
Year 2004
Volume 60
Pages 1747-52
Authors Banaszak K, Mechin I, Frost G, Rypniewski W
Title Structure of the reduced disulfide-bond isomerase DsbC from Escherichia coli.
Related PDB 1tjd
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 15057279
Journal EMBO J
Year 2004
Volume 23
Pages 1709-19
Authors Rozhkova A, Stirnimann CU, Frei P, Grauschopf U, Brunisholz R, Grutter MG, Capitani G, Glockshuber R
Title Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 15546661
Journal Biochim Biophys Acta
Year 2004
Volume 1694
Pages 111-9
Authors Nakamoto H, Bardwell JC
Title Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm.
Related PDB
Related UniProtKB

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.

Created Updated
2005-06-14 2009-02-26