dsbAdsbB
DsbADsbB refers to the bacterial disulfide-bond formation system formed by DsbA and DsbB. In many Gram-negative bacteria, this pair operates in the periplasm to catalyze the formation of disulfide bonds in exported or secreted proteins, helping them fold correctly. DsbA is a small, soluble periplasmic protein with a thioredoxin-like fold and an active-site motif, typically Cys-Gly-Tyr-Cys, that directly introduces disulfide bonds into substrate proteins. DsbB is an inner membrane protein that reoxidizes reduced DsbA after it has donated its disulfide to a substrate.
Mechanism: DsbA transfers its disulfide to a substrate, oxidizing the substrate and becoming reduced. DsbB reoxidizes
Structure and genetics: DsbA is a soluble periplasmic protein; DsbB spans the inner membrane with multiple
Biological and clinical relevance: The DsbA-DsbB system is required for proper oxidative folding of a wide