Key Players Involved in Bacterial Disulfide‐Bond Formation

Knowing when to fold. The formation of disulfide bonds, which is required for the folding and stability of many secreted proteins, is mediated by the periplasmic protein DsbA, the structure of which is shown. DsbA is kept oxidized by the inner-membrane protein DsbB. Potentially fatal aberrant disulfide bonds are corrected by the disulfide isomerases DsbC, DsbE, and DsbG, kept reduced by the membrane protein DsbD.