nDsbD: a redox interaction hub in the Escherichia coli periplasm |
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Authors: | C U Stirnimann M G Grütter R Glockshuber G Capitani |
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Institution: | 1. Biochemisches Institut, Universit?t Zürich, Winterthurerstrasse 190, 8057, Zürich, Switzerland 2. Eidgen?ssische Technische Hochschule H?nggerberg, Institut für Molekularbiologie und Biophysik, 8093, Zürich, Switzerland
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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.
Received 3 February 2006; received after revision 1 March 2006; accepted 5 April 2006 |
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Keywords: | Disulfide isomerization cytochrome c maturation DsbD DsbC DsbG CcmG |
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