This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Thiol:disulfide interchange protein
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | <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>. | ||
| - | |||
| - | |||
| - | == Function == | ||
== Disease == | == Disease == | ||
| Line 14: | Line 12: | ||
== 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
| |||||||||||
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
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky
