6qkm
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
- | '''Unreleased structure''' | ||
- | + | ==Diallyl trisulfide inhibited sulfur oxygenase reductase== | |
+ | <StructureSection load='6qkm' size='340' side='right'caption='[[6qkm]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6qkm]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QKM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QKM 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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=TSY:(2S)-2-AMINO-3-TRISULFANYLPROPANOIC+ACID'>TSY</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=6qkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qkm OCA], [http://pdbe.org/6qkm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qkm RCSB], [http://www.ebi.ac.uk/pdbsum/6qkm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qkm 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 6qkm" 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]] |
Revision as of 06:28, 19 February 2020
Diallyl trisulfide inhibited sulfur oxygenase reductase
|