Thiol:disulfide interchange protein
FunctionThiol:disulfide interchange protein (DsbC) is a prokaryotic disulfide bond isomerase.
DiseaseRelevanceStructural highlightsDsbC active site contains a CXXC motif which modulates the disulfide isomerization and protein folding in the bacterial periplasmic space[5]. |
|
3D Structures of thiol:disulfide interchange protein3D Structures of thiol:disulfide interchange protein
Updated on 12-September-2016
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
- ↑ Lundberg G, Gerdle B. Correlations between joint and spinal mobility, spinal sagittal configuration, segmental mobility, segmental pain, symptoms and disabilities in female homecare personnel. Scand J Rehabil Med. 2000 Sep;32(3):124-33. PMID:11028797