Thiol:disulfide interchange protein
From Proteopedia
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| - | <StructureSection load='1eej' size='340' side='right' caption='E. coli DsbC (PDB code [[1eej]])' scene=''> | + | <StructureSection load='1eej' size='340' side='right' caption='E. coli DsbC complex with Mes (PDB code [[1eej]])' scene=''> |
'''Thiol:disulfide interchange protein''' (DsbC) is a prokaryotic disulfide bond isomerase. 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. | '''Thiol:disulfide interchange protein''' (DsbC) is a prokaryotic disulfide bond isomerase. 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. | ||
Revision as of 09:53, 28 June 2015
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3D Structures of thiol:disulfide interchange protein
Updated on 28-June-2015
1eej, 1tjd – EcDsbC – Escherichal coli
1g0t, 1jzo – EcDsbC (mutant)
2iyj – EcDsbC N terminal
1jzd – EcDsbC (mutant) + DsbD N terminal
1t3b – DsbC – Haemophilus influenzae
4fyb, 4fyc – DsbC – Helicobacter pylori
4i5q – StDsbC – Salmonella typhimurium
4ilf – StDsbC (mutant)
References
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Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky
