Thiol:disulfide interchange protein
FunctionThiol:disulfide interchange protein is a prokaryotic disulfide bond isomerase.
Structural highlightsDsbC active site contains a which modulates the disulfide isomerization and protein folding in the bacterial periplasmic space[5][6]. 3D Structures of thiol:disulfide interchange proteinThiol:disulfide interchange protein 3D structures
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3D Structures of thiol:disulfide interchange protein3D Structures of thiol:disulfide interchange protein
Updated on 20-February-2020
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- Thiol:disulfide interchange protein (DsbA) see Protein disulfide oxidoreductase
- Thiol:disulfide interchange protein (DsbB)
- Thiol:disulfide interchange protein (DsbC)
- Thiol:disulfide interchange protein (DsbD)
- 1l6p, 1jpe, 3pfu, 5nhi – 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, 6dnv, 6dps – NmDsbD N terminal – Neisseria meningitis
- 6dnl, 6dnu – NmDsbD C terminal
- 2k9f – NmDsbD N terminal + thoredoxin
- 1l6p, 1jpe, 3pfu, 5nhi – EcDsbD N terminal
- Thiol:disulfide interchange protein (DsbE)
- Thiol:disulfide interchange protein (DsbF)
- 3ios – DsbF – Mycobacterium tuberculosis
- 3ios – DsbF – Mycobacterium tuberculosis
- Thiol:disulfide interchange protein (DsbG)
- Thiol:disulfide interchange protein (DsbP)
- Thiol:disulfide interchange protein (CycY)
- 1kng – CycY – Bradyrhizobium japonicum
- 1kng – CycY – Bradyrhizobium japonicum
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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
- ↑ 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