Thiol:disulfide interchange protein: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
Michal Harel (talk | contribs)
No edit summary
Jaime Prilusky (talk | contribs)
No edit summary
Line 49: Line 49:


**[[1v57]], [[1v58]] – EcDsbG <BR />
**[[1v57]], [[1v58]] – EcDsbG <BR />
**[[2h0g]], [[2h0h]], [[2h0i]], [[5g1k]], [[5g1l] – EcDsbG (mutant) <BR />
**[[2h0g]], [[2h0h]], [[2h0i]], [[5g1k]], [[5g1l]] – EcDsbG (mutant) <BR />
**[[2iy2]] – EcDsbG N terminal<BR />
**[[2iy2]] – EcDsbG N terminal<BR />
**[[4ihu]] – MtDsbG  <BR />
**[[4ihu]] – MtDsbG  <BR />

Revision as of 14:05, 12 September 2016

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].

E. coli DsbC complex with MES (PDB code 1eej)

Drag the structure with the mouse to rotate

3D Structures of thiol:disulfide interchange protein3D Structures of thiol:disulfide interchange protein

Updated on 12-September-2016

ReferencesReferences

  1. 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
  2. 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
  3. 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
  4. 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
  5. 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Jaime Prilusky, Joel L. Sussman