Thiol:disulfide interchange protein

Revision as of 13:43, 28 June 2015 by Michal Harel (talk | contribs)

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.
  • DsbD transfers electrons from the cytoplasmic thioredoxin to the periplasm thus maintaining the active site of DsbC, DsbE and DsbG in a reduced state.
  • DsbE catalyzes the reductive step in the assembly of periplasmic c-type cytochrome.
  • DsbG provides reducing equivalents to rescue oxidatively-damaged secreted proteins.


Function

Disease

Relevance

Structural highlights

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

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3D Structures of thiol:disulfide interchange protein3D Structures of thiol:disulfide interchange protein

Updated on 28-June-2015

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