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nDsbD: a redox interaction hub in the Escherichia coli periplasm


Stirnimann, C U; Grütter, M G; Glockshuber, R; Capitani, G (2006). nDsbD: a redox interaction hub in the Escherichia coli periplasm. Cellular and Molecular Life Sciences, 63(14):1642-1648.

Abstract

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

Abstract

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

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Item Type:Journal Article, refereed, original work
Communities & Collections:National licences > 142-005
Dewey Decimal Classification:570 Life sciences; biology
Scopus Subject Areas:Life Sciences > Molecular Medicine
Life Sciences > Molecular Biology
Life Sciences > Pharmacology
Life Sciences > Cellular and Molecular Neuroscience
Life Sciences > Cell Biology
Language:English
Date:1 July 2006
Deposited On:29 Nov 2018 16:34
Last Modified:31 Jul 2020 02:36
Publisher:Springer
ISSN:1420-682X
OA Status:Green
Publisher DOI:https://doi.org/10.1007/s00018-006-6055-1
Related URLs:https://www.swissbib.ch/Search/Results?lookfor=nationallicencespringer101007s0001800660551 (Library Catalogue)
PubMed ID:16786221

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