Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli.

Abstract excerpt

The active-site cysteines of the Escherichia coli periplasmic protein disulfide bond isomerase (DsbC) are kept reduced by the cytoplasmic membrane protein, DsbD. DsbD, in turn, is reduced by cytoplasmic thioredoxin, indicating that DsbD transfers disulfidereducing potential from the cytoplasm to the periplasm. To understand the mechanism of this unusual mode of electron transfer, we have undertaken a genetic...

Topics

• Alkaline Phosphatase
• Amino Acid Sequence
• Base Sequence
• Binding Sites
• Cysteine
• Disulfides
• Electron Transport
• Escherichia coli
• Gene Expression Regulation, Bacterial
• Gene Expression Regulation, Enzymologic