Protein disulfide oxidoreductase

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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.

3D structures of protein disulfide oxidoreductase

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 – BsResA soluble domain – Bacillus subtilis
2h19, 2h1a, 2h1b, 2h1g, 3c71, 3c73 - BsResA soluble domain (mutant)
3bci – SaDsbA – Staphylococcus aureus
3bck, 3bd2 - SaDsbA (mutant)
3gh9 - SaBdbB
3erw – SaPDOR sporulation
3fkf – PDOR – Bacterioides fragilis
2zuq - EcDsbB (mutant) + antibody

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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