6qo0
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6qo0 is ON HOLD Authors: Frazao, C., Klezin, A., Poell, U. Description: I47W mutated sulfur oxygenase reductase from Acidianus ambivaens [[Category...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==I47W mutated sulfur oxygenase reductase from Acidianus ambivaens== | |
| + | <StructureSection load='6qo0' size='340' side='right'caption='[[6qo0]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6qo0]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QO0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QO0 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sulfur_oxygenase/reductase Sulfur oxygenase/reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.55 1.13.11.55] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6qo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qo0 OCA], [http://pdbe.org/6qo0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qo0 RCSB], [http://www.ebi.ac.uk/pdbsum/6qo0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qo0 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://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> | ||
| + | <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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6qo0" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Sulfur oxygenase/reductase]] | ||
[[Category: Frazao, C]] | [[Category: Frazao, C]] | ||
| + | [[Category: Klezin, A]] | ||
[[Category: Poell, U]] | [[Category: Poell, U]] | ||
| + | [[Category: 2-his-1-carboxylate facial triad]] | ||
| + | [[Category: Biogeochemical sulfur cycle]] | ||
| + | [[Category: Cysteine persulphuration]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Sulfur oxygenase reductase]] | ||
Current revision
I47W mutated sulfur oxygenase reductase from Acidianus ambivaens
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