1st9: Difference between revisions

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{{STRUCTURE_1st9|  PDB=1st9  |  SCENE=  }}  
{{STRUCTURE_1st9|  PDB=1st9  |  SCENE=  }}  


'''Crystal Structure of a Soluble Domain of ResA in the Oxidised Form'''
===Crystal Structure of a Soluble Domain of ResA in the Oxidised Form===




==Overview==
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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.
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{{ABSTRACT_PUBMED_15047692}}


==About this Structure==
==About this Structure==
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[[Category: Soluble domain]]
[[Category: Soluble domain]]
[[Category: Thioredoxin-like domain]]
[[Category: Thioredoxin-like domain]]
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Revision as of 08:21, 29 July 2008

File:1st9.png

Template:STRUCTURE 1st9

Crystal Structure of a Soluble Domain of ResA in the Oxidised Form

Template:ABSTRACT PUBMED 15047692

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

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