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Structural basis of redox-coupled protein substrate selection by the cytochromec biosynthesis protein ResA
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Crow, Allister, Acheson, Richard M., Le Brun, Nick E. and Oubrie, Arthur (2004) Structural basis of redox-coupled protein substrate selection by the cytochromec biosynthesis protein ResA. Journal of Biological Chemistry, 279 (22). pp. 23654-23660. doi:10.1074/jbc.M402823200 ISSN 0021-9258.
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Official URL: http://dx.doi.org/10.1074/jbc.M402823200
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: | Journal Article | ||||||
|---|---|---|---|---|---|---|---|
| Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||||
| Journal or Publication Title: | Journal of Biological Chemistry | ||||||
| Publisher: | American Society for Biochemistry and Molecular Biology | ||||||
| ISSN: | 0021-9258 | ||||||
| Official Date: | 2004 | ||||||
| Dates: |
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| Volume: | 279 | ||||||
| Number: | 22 | ||||||
| Page Range: | pp. 23654-23660 | ||||||
| DOI: | 10.1074/jbc.M402823200 | ||||||
| Status: | Peer Reviewed | ||||||
| Publication Status: | Published | ||||||
| Access rights to Published version: | Restricted or Subscription Access |
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