Protein disulfide oxidoreductase
From Proteopedia
| Line 1: | Line 1: | ||
| - | {{STRUCTURE_2hi7| PDB=2hi7 | SIZE=400| SCENE= |right|CAPTION=E. coli protein disulfide peroxidase, [[2hi7]] }} | + | {{STRUCTURE_2hi7| PDB=2hi7 | SIZE=400| SCENE= |right|CAPTION=E. coli protein disulfide peroxidase complex with ubiquinone-1, [[2hi7]] }} |
<!-- | <!-- | ||
Please use the "3D" button above this box to insert a Jmol applet (molecule) on this page. | Please use the "3D" button above this box to insert a Jmol applet (molecule) on this page. | ||
Revision as of 07:14, 17 April 2012
Template:STRUCTURE 2hi7
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
