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PMID: 8521518 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Why is DsbA such an oxidizing disulfide catalyst?

Cell ·Vol. 83 ·No. 6 ·1995-12-15 ·Pages 947-55

Grauschopf U, Winther JR, Korber P, Zander T, Dallinger P, Bardwell JC

Abstract

DsbA, a member of the thioredoxin family of disulfide oxidoreductases, acts in catalyzing disulfide bond formation by donating its disulfide to newly translocated proteins. We have found that the two central residues within the active site Cys-30-Pro-31-His-32-Cys-33 motif are critical in determining the exceptional oxidizing power of DsbA. Mutations that change these two residues can alter the equilibrium oxidation potential of DsbA by more than 1000-fold. A quantitative explanation for the very high redox potential of DsbA was found by measuring the pKa of a single residue, Cys-30. The pKa of Cys-30 varied dramatically from mutant to mutant and could accurately predict the oxidizing power of each DsbA mutant protein.

MeSH Terms
Amino Acid Sequence Base Sequence Binding Sites Catalysis Cysteine/metabolism Disulfides/metabolism Enzyme Stability Isomerases/chemistry,genetics,metabolism Kinetics Molecular Sequence Data Mutation Oxidation-Reduction Oxidoreductases/chemistry,genetics,metabolism Protein Disulfide-Isomerases Protein Folding Recombinant Fusion Proteins/metabolism beta-Galactosidase/genetics,metabolism
Chemicals
Disulfides Recombinant Fusion Proteins Oxidoreductases beta-Galactosidase Isomerases Protein Disulfide-Isomerases Cysteine
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Grauschopf U
Universität Regensburg Institut für Biophysik und Physikalische Biochemie, Federal Republic of Germany.
Winther J R
Korber P
Zander T
Dallinger P
Bardwell J C
Article Info
Journal
Cell
Abbr.
Cell
ISSN
0092-8674
DOI
10.1016/0092-8674(95)90210-4
Published
1995-12-15
Pages
947-55
Language
English
Region
United States
NLM ID
0413066
Subset
IM
Databases
GENBANK
U35817, U35818, U35819, U35820, U35821, U35822, U35823, U35824, U35825, U36828, U36829, U36830, U36831, U36832, U36833, U36834, U36835
External Links
PubMed source DOI: 10.1016/0092-8674(95)90210-4 View journal details
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