Structural basis of redox-coupled protein substrate selection by the cytochrome c biosynthesis protein ResA

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Crow, Allister, Acheson, Richard M., Le Brun, Nick E. ORCID: https://orcid.org/0000-0001-9780-4061 and Oubrie, Arthur (2004) Structural basis of redox-coupled protein substrate selection by the cytochrome c biosynthesis protein ResA. Journal of Biological Chemistry, 279. pp. 23654-23660. ISSN 1083-351X

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Abstract

Post-translational maturation of cytochromes c involves the covalent attachment of heme to the Cys-Xxx-Xxx-Cys-His motif of the apo-cytochrome. For this process, the two cysteines of the motif must be in the reduced state. In bacteria, this is achieved by dedicated, membrane-bound thiol-disulfide oxidoreductases with a high reducing power, which are essential components of cytochrome c maturation systems and are also linked to cellular disulfide-bond formation machineries. Here we report high-resolution structures of oxidized and reduced states of a soluble, functional domain of one such oxidoreductase, ResA, from Bacillus subtilis. The structures elucidate the structural basis of the protein's high reducing power and reveal the largest redox-coupled conformational changes observed to date in any thioredoxin-like protein. These redox-coupled changes alter the protein surface and illustrate how the redox state of ResA predetermines to which substrate it binds. Furthermore, a polar cavity, present only in the reduced state, may confer specificity to recognize apo-cytochrome c. The described features of ResA are likely to be general for bacterial cytochrome c maturation systems.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Biological Sciences Faculty of Science > School of Chemical Sciences and Pharmacy (former - to 2009) Faculty of Science > School of Chemistry (former - to 2024)
UEA Research Groups:	Faculty of Science > Research Groups > Centre for Ocean and Atmospheric Sciences Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Chemistry of Life Processes
Related URLs:	http://www.jbc.org/content/279/22/23654
Depositing User:	Pure Connector
Date Deposited:	24 Jan 2018 17:30
Last Modified:	24 Sep 2024 10:02
URI:	https://ueaeprints.uea.ac.uk/id/eprint/66072
DOI:	10.1074/jbc.M402823200

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