The Disulfide bond oxidoreductase D (DsbD) family is a member of the Lysine Exporter (LysE) Superfamily.
[1] A representative list of proteins belonging to the DsbD family can be found in the Transporter Classification Base.
The overall vectorial electron transfer reaction catalyzed by DsbD is: 2 e−cytoplasm → 2 e−periplasm DsbB contains 4 essential cysteine residues, reversibly forming two disulfide bonds.
[11] TrxA donates electrons to the transmembrane cysteines C163 (C3) and C285 (C5) in putative TMSs 1 and 4 in the DsbD model proposed by Katzen and Beckwith (2000).
[10] This dithiol then donates electrons to the periplasmic C-terminal thioredoxin motif (CXXC) of DsbD, thereby reducing C461 and C464 (C6 and C7, respectively).