1st9
From Proteopedia
(New page: 200px<br /><applet load="1st9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1st9, resolution 1.50Å" /> '''Crystal Structure of...) |
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| - | [[Image:1st9.jpg|left|200px]]<br /><applet load="1st9" size=" | + | [[Image:1st9.jpg|left|200px]]<br /><applet load="1st9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1st9, resolution 1.50Å" /> | caption="1st9, resolution 1.50Å" /> | ||
'''Crystal Structure of a Soluble Domain of ResA in the Oxidised Form'''<br /> | '''Crystal Structure of a Soluble Domain of ResA in the Oxidised Form'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Post-translational maturation of cytochromes c involves the covalent | + | 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== | ==About this Structure== | ||
| - | 1ST9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with EDO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1ST9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ST9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Acheson, R | + | [[Category: Acheson, R M.]] |
| - | [[Category: Brun, N | + | [[Category: Brun, N E.Le.]] |
[[Category: Crow, A.]] | [[Category: Crow, A.]] | ||
[[Category: Oubrie, A.]] | [[Category: Oubrie, A.]] | ||
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[[Category: thioredoxin-like domain]] | [[Category: thioredoxin-like domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:04:59 2008'' |
Revision as of 13:05, 21 February 2008
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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 with as ligand. 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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