Thiol:disulfide interchange protein

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.

Function

Disease

Relevance

Structural highlights

3D Structures of thiol:disulfide interchange protein3D 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)

ReferencesReferences

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Jaime Prilusky, Joel L. Sussman