Function
Thiol:disulfide interchange protein is a prokaryotic disulfide bond isomerase.
- DsbA see Protein disulfide oxidoreductase
- DsbC acts as a proofreader and breaks the incorrectly formed disulfide bonds. DsbC is activated by the N terminal domain of DsbD[1].
- DsbD transfers electrons from the cytoplasmic thioredoxin to the periplasm thus maintaining the active site of DsbC, DsbE and DsbG in a reduced state[2].
- DsbE catalyzes the reductive step in the assembly of periplasmic c-type cytochrome[3].
- DsbG provides reducing equivalents to rescue oxidatively-damaged secreted proteins[4].
Structural highlights
DsbC active site contains a CXXC motif which modulates the disulfide isomerization and protein folding in the bacterial periplasmic space[5][6].
3D Structures of thiol:disulfide interchange protein
Thiol:disulfide interchange protein 3D structures
- ↑ 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:https://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:https://dx.doi.org/10.1128/JB.183.3.980-988.2001
