1st9: Difference between revisions

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{{Seed}}
[[Image:1st9.png|left|200px]]


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==Crystal Structure of a Soluble Domain of ResA in the Oxidised Form==
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<StructureSection load='1st9' size='340' side='right'caption='[[1st9]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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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<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>
{{STRUCTURE_1st9|  PDB=1st9  |  SCENE=  }}
<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>
</table>
== Function ==
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/st/1st9_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
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.


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


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1st9" style="background-color:#fffaf0;"></div>


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==See Also==
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*[[Protein disulfide oxidoreductase 3D structures|Protein disulfide oxidoreductase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 15047692 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_15047692}}
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</StructureSection>
==About this Structure==
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].
 
==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:[http://www.ncbi.nlm.nih.gov/pubmed/15047692 15047692]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Acheson, R M.]]
[[Category: Acheson RM]]
[[Category: Brun, N E.Le.]]
[[Category: Crow A]]
[[Category: Crow, A.]]
[[Category: Le Brun NE]]
[[Category: Oubrie, A.]]
[[Category: Oubrie A]]
[[Category: Alpha-beta protein]]
[[Category: Membrane protein]]
[[Category: Soluble domain]]
[[Category: Thioredoxin-like domain]]
 
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Retrieved from "https://proteopedia.org/1st9"