1st9
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= RESA, BSU23150 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | |GENE= RESA, BSU23150 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1su9|1SU9]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1st9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1st9 OCA], [http://www.ebi.ac.uk/pdbsum/1st9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1st9 RCSB]</span> | ||
}} | }} | ||
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[[Category: Crow, A.]] | [[Category: Crow, A.]] | ||
[[Category: Oubrie, A.]] | [[Category: Oubrie, A.]] | ||
| - | [[Category: EDO]] | ||
[[Category: alpha-beta protein]] | [[Category: alpha-beta protein]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
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[[Category: thioredoxin-like domain]] | [[Category: thioredoxin-like domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:46:40 2008'' |
Revision as of 20:46, 30 March 2008
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| , resolution 1.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | RESA, BSU23150 (Bacillus subtilis) | ||||||
| Related: | 1SU9
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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