Thiol:disulfide interchange protein (DsbC) is a prokaryotic disulfide bond isomerase.
- DsbC acts as a proofreader and breaks the incorrectly formed disulfide bonds. It contains the CXXC motif. DsbC is activated by the N terminal domain of DsbD.
- DsbD transfers electrons from the cytoplasmic thioredoxin to the periplasm thus maintaining the active site of DsbC, DsbE and DsbG in a reduced state.
- DsbE catalyzes the reductive step in the assembly of periplasmic c-type cytochrome.
- DsbG provides reducing equivalents to rescue oxidatively-damaged secreted proteins.
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