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[[Image:2cb2.gif|left|200px]]<br /><applet load="2cb2" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2cb2, resolution 1.70&Aring;" />
'''SULFUR OXYGENASE REDUCTASE FROM ACIDIANUS AMBIVALENS'''<br />


==Overview==
==Sulfur Oxygenase Reductase from Acidianus Ambivalens==
Numerous microorganisms oxidize sulfur for energy conservation and, contribute to the global biogeochemical sulfur cycle. We have determined, the 1.7 angstrom-resolution structure of the sulfur oxygenase reductase, from the thermoacidophilic archaeon Acidianus ambivalens, which catalyzes, an oxygen-dependent disproportionation of elemental sulfur. Twenty-four, monomers form a large hollow sphere enclosing a positively charged, nanocompartment. Apolar channels provide access for linear sulfur species., A cysteine persulfide and a low-potential mononuclear non-heme iron site, ligated by a 2-His-1-carboxylate facial triad in a pocket of each subunit, constitute the active sites, accessible from the inside of the sphere. The, iron is likely the site of both sulfur oxidation and sulfur reduction.
<StructureSection load='2cb2' size='340' side='right'caption='[[2cb2]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2cb2]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidianus_ambivalens Acidianus ambivalens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CB2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cb2 OCA], [https://pdbe.org/2cb2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cb2 RCSB], [https://www.ebi.ac.uk/pdbsum/2cb2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cb2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SOR_ACIAM SOR_ACIAM] Catalyzes the simultaneous oxidation and reduction of elemental sulfur in the presence of oxygen, with sulfite and hydrogen sulfide as products.<ref>PMID:15030315</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/cb/2cb2_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2cb2 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Numerous microorganisms oxidize sulfur for energy conservation and contribute to the global biogeochemical sulfur cycle. We have determined the 1.7 angstrom-resolution structure of the sulfur oxygenase reductase from the thermoacidophilic archaeon Acidianus ambivalens, which catalyzes an oxygen-dependent disproportionation of elemental sulfur. Twenty-four monomers form a large hollow sphere enclosing a positively charged nanocompartment. Apolar channels provide access for linear sulfur species. A cysteine persulfide and a low-potential mononuclear non-heme iron site ligated by a 2-His-1-carboxylate facial triad in a pocket of each subunit constitute the active sites, accessible from the inside of the sphere. The iron is likely the site of both sulfur oxidation and sulfur reduction.


==About this Structure==
X-ray Structure of a self-compartmentalizing sulfur cycle metalloenzyme.,Urich T, Gomes CM, Kletzin A, Frazao C Science. 2006 Feb 17;311(5763):996-1000. PMID:16484493<ref>PMID:16484493</ref>
2CB2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acidianus_ambivalens Acidianus ambivalens] with <scene name='pdbligand=FE:'>FE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Fe+Binding+Site+For+Chain+F'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CB2 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
X-ray Structure of a self-compartmentalizing sulfur cycle metalloenzyme., Urich T, Gomes CM, Kletzin A, Frazao C, Science. 2006 Feb 17;311(5763):996-1000. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16484493 16484493]
</div>
<div class="pdbe-citations 2cb2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Acidianus ambivalens]]
[[Category: Acidianus ambivalens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Frazao, C.]]
[[Category: Frazao C]]
[[Category: Gomes, C.M.]]
[[Category: Gomes CM]]
[[Category: Kletzin, A.]]
[[Category: Kletzin A]]
[[Category: Urich, T.]]
[[Category: Urich T]]
[[Category: FE]]
[[Category: 2-his-1-carboxylate facial triad]]
[[Category: acidophilic]]
[[Category: archaea]]
[[Category: biogeochemical sulfur cycle]]
[[Category: compartmentalization]]
[[Category: cysteine persulphide]]
[[Category: extremophile]]
[[Category: icosatetramer]]
[[Category: metal-binding]]
[[Category: mononuclear non-heme iron]]
[[Category: nano-structure]]
[[Category: oxidoreductase]]
[[Category: proto-organelle]]
[[Category: sulfur oxygenase reductase]]
[[Category: thermophilic]]
 
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