Article
Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.
Journal of bacteriology - 1 Nov 1997
Rietsch A, Bessette P, Georgiou G, Beckwith J
Abstract excerpt
The Escherichia coli periplasmic protein DsbC is active both in vivo and in vitro as a protein disulfide isomerase. For DsbC to attack incorrectly formed disulfide bonds in substrate proteins, its two active-site cysteines should be in the reduced form. Here we present evidence that, in wild-type...
Topics
- Aprotinin
- Binding Sites
- Cell Compartmentation
- Cysteine
- Cytoplasm
- Electron Transport
- Escherichia coli
- Glutathione Reductase
- Models, Molecular
- Mutation
- Periplasm
- Protein Disulfide-Isomerases
- Protein Folding
- Thioredoxin-Disulfide Reductase
- Thioredoxins
- Urokinase-Type Plasminogen Activator