Function
Protein disulfide oxidoreductase (PDOR) catalyzes disulfide bond formation in proteins and is critically important in protein folding. In bacteria PDOR are known as DsbA and DsbB. PDOR catalyze dithiol-disulfide exchange reactions, i.e., conversion of RSSR and R’SH to R’SSR’ and RSH[1].
Structural highlights
PDOR DsnA contains the in the active site. The 2 cysteines can undergo reversible oxidation-reduction in the catalytic process[2].
3D structures of protein disulfide oxidoreductase
Protein disulfide oxidoreductase 3D structures
For DsbB see Thiol:disulfide interchange protein.
References
- ↑ Pedone E, Ren B, Ladenstein R, Rossi M, Bartolucci S. Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus: a member of a novel protein family related to protein disulfide-isomerase. Eur J Biochem. 2004 Aug;271(16):3437-48. PMID:15291821 doi:http://dx.doi.org/10.1111/j.0014-2956.2004.04282.x
- ↑ Heras B, Kurz M, Jarrott R, Byriel KA, Jones A, Thony-Meyer L, Martin JL. Expression and crystallization of DsbA from Staphylococcus aureus. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Nov 1;63(Pt, 11):953-6. Epub 2007 Oct 24. PMID:18007049 doi:10.1107/S174430910704821X
