Protein disulfide oxidoreductase

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Template:STRUCTURE 2hi7

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. PDOR contains the sequence CXXC in the active site. The 2 cysteines can undergo reversible oxidation-reduction in the catalytic process^[1].

3D structures of protein disulfide oxidoreductase

Updated on 14-July-2016

1a8l – PDOR – Pyrococcus furiosus
1bq7 – EcDsbA (mutant) – Escherichia coli
2hi7, 3e9j, 2zup - EcDsbA (mutant) + EcDsbB (mutant)
2leg - EcDsbA (mutant) + EcDsbB (mutant) - NMR
2k73, 2k74 - EcDsbB (mutant) - NMR
1fo5 – PDOR – Methanocaldococcus jannaschii – NMR
2ayt – PDOR – Aquifex aeolicus
2hls – PDOR – Aeropyrus pernix
2rem - DsbA + peptide – Xylella fastidiosa
1st9, 1su9, 2f9s, 2h1d, 3gha – BsResA soluble domain – Bacillus subtilis
3eu3 – BsBdbB
2h19, 2h1a, 2h1b, 2h1g, 3c71, 3c73 - BsResA soluble domain (mutant)
4k6x – PDOR – Mycobacterium tuberculosis
3bci – SaDsbA – Staphylococcus aureus
3bck, 3bd2 - SaDsbA (mutant)
3gh9 - SaBdbB
3erw – SaPDOR sporulation
3fkf – PDOR – Bacterioides fragilis
1bed – DsbA – Vibrio cholerae
2zuq, 2ltq - EcDsbB (mutant) + antibody

References

1. ↑ 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