Thiol:disulfide interchange protein
From Proteopedia
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| - | <StructureSection load='1eej' size='340' side='right' caption='E. coli DsbC complex with | + | <StructureSection load='1eej' size='340' side='right' caption='E. coli DsbC complex with MES (PDB code [[1eej]])' scene=''> |
| + | == Function == | ||
'''Thiol:disulfide interchange protein''' (DsbC) is a prokaryotic disulfide bond isomerase. <br /> | '''Thiol:disulfide interchange protein''' (DsbC) is a prokaryotic disulfide bond isomerase. <br /> | ||
| - | *'''DsbC''' acts as a proofreader and breaks the incorrectly formed disulfide bonds | + | *'''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 /> |
*'''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 /> | *'''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 /> | ||
*'''DsbE''' catalyzes the reductive step in the assembly of periplasmic c-type cytochrome<ref>PMID:14597624</ref>. <br /> | *'''DsbE''' catalyzes the reductive step in the assembly of periplasmic c-type cytochrome<ref>PMID:14597624</ref>. <br /> | ||
*'''DsbG''' provides reducing equivalents to rescue oxidatively-damaged secreted proteins<ref>PMID:9654144</ref>. | *'''DsbG''' provides reducing equivalents to rescue oxidatively-damaged secreted proteins<ref>PMID:9654144</ref>. | ||
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| - | == Function == | ||
== Disease == | == Disease == | ||
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== Structural highlights == | == Structural highlights == | ||
| - | + | DsbC active site contains a CXXC motif which modulates the disulfide isomerization and protein folding in the bacterial periplasmic space<ref>PMID:11028797</ref>. | |
</StructureSection> | </StructureSection> | ||
Revision as of 07:47, 12 September 2016
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3D Structures of thiol:disulfide interchange protein
Updated on 12-September-2016
References
- ↑ 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
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