1st9
From Proteopedia
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'''Crystal Structure of a Soluble Domain of ResA in the Oxidised Form''' | '''Crystal Structure of a Soluble Domain of ResA in the Oxidised Form''' | ||
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[[Category: Crow, A.]] | [[Category: Crow, A.]] | ||
[[Category: Oubrie, A.]] | [[Category: Oubrie, A.]] | ||
| - | [[Category: | + | [[Category: Alpha-beta protein]] |
| - | [[Category: | + | [[Category: Membrane protein]] |
| - | [[Category: | + | [[Category: Soluble domain]] |
| - | [[Category: | + | [[Category: Thioredoxin-like domain]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:06:57 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:06, 3 May 2008
Crystal Structure of a Soluble Domain of ResA in the Oxidised Form
Overview
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.
About this Structure
1ST9 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Structural basis of Redox-coupled protein substrate selection by the cytochrome c biosynthesis protein ResA., Crow A, Acheson RM, Le Brun NE, Oubrie A, J Biol Chem. 2004 May 28;279(22):23654-60. Epub 2004 Mar 26. PMID:15047692 Page seeded by OCA on Sat May 3 09:06:57 2008
