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Molecular basis for specificity of the extracytoplasmic thioredoxin ResA
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Lewin, Allison, Crow, Allister, Oubrie, Arthur and Le Brun, Nick E. (2006) Molecular basis for specificity of the extracytoplasmic thioredoxin ResA. Journal of Biological Chemistry, 281 (46). pp. 35467-35477. doi:10.1074/jbc.M607047200 ISSN 0021-9258.
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Official URL: http://dx.doi.org/10.1074/jbc.M607047200
Abstract
ResA, an extracytoplasmic thioredoxin from Bacillus subtilis, acts in cytochrome c maturation by reducing the disulfide bond present in apocytochromes prior to covalent attachment of heme. This reaction is (and has to be) specific, as broad substrate specificity would result in unproductive shortcircuiting with the general oxidizing thioredoxin(s) present in the same compartment. Using mutational analysis and subsequent biochemical and structural characterization of active site variants, we show that reduced ResA displays unusually low reactivity at neutral pH, consistent with the observed high pKa values >8 for both active site cysteines. Residue Glu80 is shown to play a key role in controlling the acid-base properties of the active site. A model in which substrate binding dramatically enhances the reactivity of the active site cysteines is proposed to account for the specificity of the protein. Such a substratemediated activation mechanism is likely to have wide relevance for extracytoplasmic thioredoxins.
| 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: | September 2006 | ||||||
| Dates: |
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| Volume: | 281 | ||||||
| Number: | 46 | ||||||
| Page Range: | pp. 35467-35477 | ||||||
| DOI: | 10.1074/jbc.M607047200 | ||||||
| Status: | Peer Reviewed | ||||||
| Publication Status: | Published | ||||||
| Access rights to Published version: | Open Access (Creative Commons) |
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