1su9

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[[Image:1su9.jpg|left|200px]]
[[Image:1su9.jpg|left|200px]]
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{{Structure
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|PDB= 1su9 |SIZE=350|CAPTION= <scene name='initialview01'>1su9</scene>, resolution 1.95&Aring;
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|GENE= RESA, BSU23150 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
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{{STRUCTURE_1su9| PDB=1su9 | SCENE= }}
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|RELATEDENTRY=[[1st9|1ST9]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1su9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1su9 OCA], [http://www.ebi.ac.uk/pdbsum/1su9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1su9 RCSB]</span>
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'''Reduced structure of the soluble domain of ResA'''
'''Reduced structure of the soluble domain of ResA'''
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[[Category: Crow, A.]]
[[Category: Crow, A.]]
[[Category: Oubrie, A.]]
[[Category: Oubrie, A.]]
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[[Category: alpha-beta protein]]
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[[Category: Alpha-beta protein]]
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[[Category: membrane protein]]
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[[Category: Membrane protein]]
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[[Category: soluble domain]]
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[[Category: Soluble domain]]
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[[Category: thioredoxin-like domain]]
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[[Category: Thioredoxin-like domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:08:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:47:00 2008''
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Revision as of 06:08, 3 May 2008

Template:STRUCTURE 1su9

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 Page seeded by OCA on Sat May 3 09:08:32 2008

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