Protein disulfide oxidoreductase

From Proteopedia

spinqualitylabelsall models DsbA (PDB entry 3bci) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Structural highlights 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

Updated on 08-October-2020

1a8l – PDOR – Pyrococcus furiosus
1bq7 – EcDsbA (mutant) – Escherichia coli
2hi7, 3e9j, 2zup - EcDsbA (mutant) + EcDsbB (mutant)
2leg - EcDsbA (mutant) + 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
4z7x - PDOR - Actinomyces oris
5cnw, 5e59 - DrPDOR - Deinicoccus radiodurans
5cp1 - DrPDOR (mutant)
4mcu - PDOR - Klebsiella pneumoniae
4oce - PDOR - Proteus mirabillis
4jrr - DsbA1 - Legionella pneumophila
For DsbB see Thiol:disulfide interchange protein.

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
2. ↑ 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