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Cellular and Molecular Life Sciences CMLS

, Volume 63, Issue 14, pp 1642–1648 | Cite as

nDsbD: a redox interaction hub in the Escherichia coli periplasm

  • C. U. Stirnimann
  • M. G. GrütterEmail author
  • R. Glockshuber
  • G. CapitaniEmail author
Review

Abstract.

DsbD is a redox-active protein of the inner Escherichia coli membrane possessing an N-terminal (nDsbD) and a C-terminal (cDsbD) periplasmic domain. nDsbD interacts with four different redox proteins involved in the periplasmic disulfide isomerization and in the cytochrome c maturation systems. We review here the studies that led to the structural characterization of all soluble DsbD domains involved and, most importantly, of trapped disulfide intermediate complexes of nDsbD with three of its four redox partners. These results revealed the structural features enabling nDsbD, a ‘redox hub’ with an immunoglobulin-like fold, to interact efficiently with its different thioredoxin-like partners.

Keywords.

Disulfide isomerization cytochrome c maturation DsbD DsbC DsbG CcmG 

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Copyright information

© Birkhäuser Verlag, Basel 2006

Authors and Affiliations

  1. 1.Biochemisches InstitutUniversität ZürichZürichSwitzerland
  2. 2.Eidgenössische Technische Hochschule HönggerbergInstitut für Molekularbiologie und BiophysikZürichSwitzerland

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