Thiol:disulfide interchange protein: Difference between revisions

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<StructureSection load='' size='340' side='right' caption='E. coli DsbC complex with MES (PDB code [[1eej]])' scene='70/705687/Cv/1'>
<StructureSection load='' size='340' side='right' caption='E. coli DsbC complex with MES (PDB code [[1eej]])' scene='70/705687/Cv/1'>
__TOC__
== Function ==
== Function ==
'''Thiol:disulfide interchange protein''' is a prokaryotic disulfide bond isomerase.  <br />
'''Thiol:disulfide interchange protein''' is a prokaryotic disulfide bond isomerase.  <br />
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</StructureSection>
</StructureSection>
== 3D Structures of thiol:disulfide interchange protein ==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
*Thiol:disulfide interchange protein (DsbA) see [[Protein disulfide oxidoreductase]]
* Thiol:disulfide interchange protein (DsbB)
**[[3e9j], [[2zup]]] – EcDsbB (mutant) + DsbA (mutant) - ''Escherichal coli''  <BR />
**[[2leg]]] – EcDsbB (mutant) + DsbA (mutant) - NMR<BR />
**[[2hi7]]] – EcDsbB (mutant) + DsbA (mutant) + ubiquinone <BR />
**[[2zuq]] – EcDsbB (mutant) + antibody<BR />
*Thiol:disulfide interchange protein (DsbC)
**[[1eej]], [[1tjd]] – EcDsbC  <BR />
**[[1g0t]], [[1jzo]] – EcDsbC (mutant) <BR />
**[[2iyj]] – EcDsbC N terminal<BR />
**[[1jzd]] – EcDsbC (mutant) + DsbD N terminal<BR />
**[[1t3b]] – DsbC – ''Haemophilus influenzae'' <BR />
**[[4fyb]], [[4fyc]] – HpDsbC – ''Helicobacter pylori'' <BR />
**[[4i5q]] – StDsbC – ''Salmonella typhimurium''<BR />
**[[4ilf]] – StDsbC (mutant) <BR />
**[[4npb]] – DsbC –'' Yersinia pestis'' <BR />
*Thiol:disulfide interchange protein (DsbD)
**[[1l6p]], [[1jpe]], [[3pfu]], [[5nhi]] – EcDsbD N terminal<BR />
**[[1uc7]], [[2fwe]], [[2fwf]] [[2fwg]], [[2fwh]] – EcDsbD C terminal<BR />
**[[4ip1]], [[4ip6]] – EcDsbD C terminal (mutant)<BR />
**[[1vrs]] – EcDsbD N terminal (mutant) + C terminal (mutant)<BR />
**[[1z5y]] – EcDsbD N terminal (mutant) + EcDsbE soluble domain (mutant)<BR />
**[[2k0r]], [[6dnv]], [[6dps]] – NmDsbD N terminal – ''Neisseria meningitis''<BR />
**[[6dnl]], [[6dnu]] – NmDsbD C terminal <BR />
**[[2k9f]] – NmDsbD N terminal + thoredoxin<BR />
*Thiol:disulfide interchange protein (DsbE)
**[[2b1k]], [[3k8n]] – EcDsbE <BR />
**[[2b1l]], [[2g0f]] – EcDsbE (mutant) <BR />
**[[3kh7]], [[3kh9]] – DsbE soluble domain – ''Pseudomonas aeruginosa''<BR />
*Thiol:disulfide interchange protein (DsbF)
**[[3ios]] – DsbF – ''Mycobacterium tuberculosis'' <BR />
*Thiol:disulfide interchange protein (DsbG)
**[[1v57]], [[1v58]] – EcDsbG <BR />
**[[2h0g]], [[2h0h]], [[2h0i]], [[5g1k]], [[5g1l]] – EcDsbG (mutant) <BR />
**[[2iy2]] – EcDsbG N terminal<BR />
**[[4ihu]] – MtDsbG  <BR />
**[[3tdg]] – HpDsbG<BR />
*Thiol:disulfide interchange protein (DsbP)
**[[4ml1]], [[4ml6]], [[4mly]] – DsbP – ''Klebsiella pneumoniae'' <BR />
*Thiol:disulfide interchange protein (CycY)
**[[1kng]] – CycY – ''Bradyrhizobium japonicum'' <BR />
}}


== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 13:29, 20 February 2020

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 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


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

Drag the structure with the mouse to rotate

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
  6. ↑ 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

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