Thiol:disulfide interchange protein
FunctionThiol:disulfide interchange protein is a prokaryotic disulfide bond isomerase.
Structural highlightsDsbC active site contains a CXXC motif which modulates the disulfide isomerization and protein folding in the bacterial periplasmic space[5]. |
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3D Structures of thiol:disulfide interchange protein3D Structures of thiol:disulfide interchange protein
Updated on 12-September-2016 {{#tree:id=OrganizedByTopic|openlevels=0|
- Thiol:disulfide interchange protein (DsbC)
- 1eej, 1tjd – EcDsbC – Escherichal coli
- 1g0t, 1jzo – EcDsbC (mutant)
- 2iyj – EcDsbC N terminal
- 1jzd – EcDsbC (mutant) + DsbD N terminal
- 1t3b – DsbC – Haemophilus influenzae
- 4fyb, 4fyc – HpDsbC – Helicobacter pylori
- 4i5q – StDsbC – Salmonella typhimurium
- 4ilf – StDsbC (mutant)
- 4npb – DsbC – Yersinia pestis
- 1eej, 1tjd – EcDsbC – Escherichal coli
- Thiol:disulfide interchange protein (DsbD)
- 1l6p, 1jpe, 3pfu – EcDsbD N terminal
- 1uc7, 2fwe, 2fwf 2fwg, 2fwh – EcDsbD C terminal
- 4ip1, 4ip6 – EcDsbD C terminal (mutant)
- 1vrs – EcDsbD N terminal (mutant) + C terminal (mutant)
- 1z5y – EcDsbD N terminal (mutant) + EcDsbE soluble domain (mutant)
- 2k0r – NmDsbD N terminal – Neisseria meningitis
- 2k9f – NmDsbD N terminal + thoredoxin
- 1l6p, 1jpe, 3pfu – EcDsbD N terminal
- Thiol:disulfide interchange protein (DsbE)
- Thiol:disulfide interchange protein (DsbG)
- Thiol:disulfide interchange protein (DsbP)
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ReferencesReferences
- ↑ Rietsch A, Bessette P, Georgiou G, Beckwith J. Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. J Bacteriol. 1997 Nov;179(21):6602-8. PMID:9352906
- ↑ Chung J, Chen T, Missiakas D. Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm. Mol Microbiol. 2000 Mar;35(5):1099-109. PMID:10712691
- ↑ Goulding CW, Apostol MI, Gleiter S, Parseghian A, Bardwell J, Gennaro M, Eisenberg D. Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosis. J Biol Chem. 2004 Jan 30;279(5):3516-24. Epub 2003 Nov 3. PMID:14597624 doi:10.1074/jbc.M311833200
- ↑ van Straaten M, Missiakas D, Raina S, Darby NJ. The functional properties of DsbG, a thiol-disulfide oxidoreductase from the periplasm of Escherichia coli. FEBS Lett. 1998 May 29;428(3):255-8. PMID:9654144
- ↑ Bessette PH, Qiu J, Bardwell JC, Swartz JR, Georgiou G. Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli. J Bacteriol. 2001 Feb;183(3):980-8. PMID:11208797 doi:http://dx.doi.org/10.1128/JB.183.3.980-988.2001