1st9

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[[Image:1st9.jpg|left|200px]]
 
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{{Structure
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==Crystal Structure of a Soluble Domain of ResA in the Oxidised Form==
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|PDB= 1st9 |SIZE=350|CAPTION= <scene name='initialview01'>1st9</scene>, resolution 1.50&Aring;
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<StructureSection load='1st9' size='340' side='right'caption='[[1st9]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
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<table><tr><td colspan='2'>[[1st9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ST9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ST9 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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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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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1st9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1st9 OCA], [https://pdbe.org/1st9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1st9 RCSB], [https://www.ebi.ac.uk/pdbsum/1st9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1st9 ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1su9|1SU9]]
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</table>
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|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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== Function ==
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}}
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[https://www.uniprot.org/uniprot/RESA_BACSU RESA_BACSU] Thiol-disulfide oxidoreductase which is required in disulfide reduction during c-type cytochrome synthesis. May accept reducing equivalents from CcdA, leading to breakage of disulfide bonds in apocytochrome c; following this reduction heme can be covalently attached. Does not play a role in sporulation.<ref>PMID:12637552</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/st/1st9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1st9 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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'''Crystal Structure of a Soluble Domain of ResA in the Oxidised Form'''
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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<ref>PMID:15047692</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1st9" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Protein disulfide oxidoreductase 3D structures|Protein disulfide oxidoreductase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1ST9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ST9 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15047692 15047692]
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Acheson, R M.]]
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[[Category: Acheson RM]]
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[[Category: Brun, N E.Le.]]
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[[Category: Crow A]]
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[[Category: Crow, A.]]
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[[Category: Le Brun NE]]
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[[Category: Oubrie, A.]]
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[[Category: Oubrie A]]
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[[Category: alpha-beta protein]]
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[[Category: membrane protein]]
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[[Category: soluble domain]]
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[[Category: thioredoxin-like domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:46:40 2008''
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Current revision

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

PDB ID 1st9

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