Thiol:disulfide interchange protein

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<StructureSection load='1eej' size='340' side='right' caption='E. coli DsbC complex with Mes (PDB code [[1eej]])' scene=''>
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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'>
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'''Thiol:disulfide interchange protein''' (DsbC) is a prokaryotic disulfide bond isomerase. <br />
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__TOC__
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*'''DsbC''' acts as a proofreader and breaks the incorrectly formed disulfide bonds. It contains the CXXC motif. DsbC is activated by the N terminal domain of DsbD.<br />
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*'''DsbD''' transfers electrons from the cytoplasmic thioredoxin to the periplasm thus maintaining the active site of DsbC, DsbE and DsbG in a reduced state.<br />
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*'''DsbE''' catalyzes the reductive step in the assembly of periplasmic c-type cytochrome. <br />
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*'''DsbG''' provides reducing equivalents to rescue oxidatively-damaged secreted proteins.
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== Function ==
== Function ==
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'''Thiol:disulfide interchange protein''' is a prokaryotic disulfide bond isomerase. <br />
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== Disease ==
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*'''DsbA''' see [[Protein disulfide oxidoreductase]]<br />
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*'''DsbC''' acts as a proofreader and breaks the incorrectly formed disulfide bonds. DsbC is activated by the N terminal domain of DsbD<ref>PMID:9352906</ref>.<br />
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== Relevance ==
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*'''DsbD''' transfers electrons from the cytoplasmic thioredoxin to the periplasm thus maintaining the active site of DsbC, DsbE and DsbG in a reduced state<ref>PMID:10712691</ref>.<br />
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*'''DsbE''' catalyzes the reductive step in the assembly of periplasmic c-type cytochrome<ref>PMID:14597624</ref>. <br />
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*'''DsbG''' provides reducing equivalents to rescue oxidatively-damaged secreted proteins<ref>PMID:9654144</ref>.
== Structural highlights ==
== Structural highlights ==
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DsbC active site contains a <scene name='70/705687/Cv/2'>CXXC motif</scene> which modulates the disulfide isomerization and protein folding in the bacterial periplasmic space<ref>PMID:11208797</ref><ref>PMID:11208797</ref>.
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== 3D Structures of thiol:disulfide interchange protein ==
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[[Thiol:disulfide interchange protein 3D structures]]
</StructureSection>
</StructureSection>
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== 3D Structures of thiol:disulfide interchange protein ==
 
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
 
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{{#tree:id=OrganizedByTopic|openlevels=0|
 
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* Thiol:disulfide interchange protein (DsbC)
 
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**[[1eej]], [[1tjd]] – EcDsbC – ''Escherichal coli'' <BR />
 
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**[[1g0t]], [[1jzo]] – EcDsbC (mutant) <BR />
 
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**[[2iyj]] – EcDsbC N terminal<BR />
 
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**[[1jzd]] – EcDsbC (mutant) + DsbD N terminal<BR />
 
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**[[1t3b]] – DsbC – ''Haemophilus influenzae'' <BR />
 
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**[[4fyb]], [[4fyc]] – DsbC – ''Helicobacter pylori'' <BR />
 
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**[[4i5q]] – StDsbC – ''Salmonella typhimurium''<BR />
 
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**[[4ilf]] – StDsbC (mutant) <BR />
 
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*Thiol:disulfide interchange protein (DsbD)
 
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**[[1l6p]], [[1jpe]], [[3pfu]] – EcDsbD N terminal<BR />
 
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**[[1uc7]], [[2fwe]], [[2fwf]] [[2fwg]], [[2fwh]] – EcDsbD C terminal<BR />
 
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**[[4ip1]], [[4ip6]] – EcDsbD C terminal (mutant)<BR />
 
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**[[1vrs]] – EcDsbD N terminal (mutant) + C terminal (mutant)<BR />
 
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**[[1z5y]] – EcDsbD N terminal (mutant) + EcDsbE soluble domain (mutant)<BR />
 
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**[[2k0r]] – NmDsbD N terminal – ''Neisseria meningitis''<BR />
 
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**[[2k9f]] – NmDsbD N terminal + thoredoxin<BR />
 
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*Thiol:disulfide interchange protein (DsbE)
 
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**[[2b1k]], [[3k8n]] – EcDsbE <BR />
 
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**[[2b1l]], [[2g0f]] – EcDsbE (mutant) <BR />
 
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**[[3kh7]], [[3kh9]] – DsbE soluble domain – ''Pseudomonas aeruginosa''<BR />
 
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*Thiol:disulfide interchange protein (DsbG)
 
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**[[1v57]], [[1v58]] – EcDsbG <BR />
 
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**[[2h0g]], [[2h0h]], [[2h0i]] – EcDsbG (mutant) <BR />
 
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**[[2iy2]] – EcDsbG N terminal<BR />
 
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}}
 
== References ==
== References ==
<references/>
<references/>
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[[Category:Topic Page]]

Current revision

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

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References

  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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