1su9 | pdb_00001su9
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Reduced structure of the soluble domain of ResA
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
1SU9 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
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