Protein disulfide oxidoreductase
From Proteopedia
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{{STRUCTURE_2hi7| PDB=2hi7 | SIZE=400| SCENE= |right|CAPTION=E. coli DsbA (grey) and DsbB (green) complex with ubiquinone and Zn+2 ion (grey), [[2hi7]] }} | {{STRUCTURE_2hi7| PDB=2hi7 | SIZE=400| SCENE= |right|CAPTION=E. coli DsbA (grey) and DsbB (green) complex with ubiquinone and Zn+2 ion (grey), [[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<ref>PMID:15291821</ref>. | |
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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== | ==3D structures of protein disulfide oxidoreductase== | ||
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[[3gh9]] - SaBdbB<br /> | [[3gh9]] - SaBdbB<br /> | ||
[[3erw]] – SaPDOR sporulation<br /> | [[3erw]] – SaPDOR sporulation<br /> | ||
| - | [[3fkf]] – PDOR – Bacterioides fragilis<br /> | + | [[3fkf]] – PDOR – ''Bacterioides fragilis''<br /> |
[[1bed]] – DsbA – ''Vibrio cholerae''<br /> | [[1bed]] – DsbA – ''Vibrio cholerae''<br /> | ||
[[2zuq]], [[2ltq]] - EcDsbB (mutant) + antibody | [[2zuq]], [[2ltq]] - EcDsbB (mutant) + antibody | ||
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| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 07:58, 14 July 2016
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
- ↑ 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
