6qkm

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'''Unreleased structure'''
 
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The entry 6qkm is ON HOLD until Paper Publication
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==Diallyl trisulfide inhibited sulfur oxygenase reductase==
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<StructureSection load='6qkm' size='340' side='right'caption='[[6qkm]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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<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>
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<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>
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</table>
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== Function ==
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[[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Frazao, C., Klezin, A., Poell, U.
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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>
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Description: Diallyl trisulfide inhibited sulfur oxygenase reductase
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Klezin, A]]
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<div class="pdbe-citations 6qkm" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Sulfur oxygenase/reductase]]
[[Category: Frazao, C]]
[[Category: Frazao, C]]
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[[Category: Klezin, A]]
[[Category: Poell, U]]
[[Category: Poell, U]]
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[[Category: 2-his-1-carboxylate facial triad]]
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[[Category: Biogeochemical sulfur cycle]]
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[[Category: Cysteine persulphuration]]
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[[Category: Oxidoreductase]]
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[[Category: Sulfur oxygenase reductase]]

Revision as of 06:28, 19 February 2020

Diallyl trisulfide inhibited sulfur oxygenase reductase

PDB ID 6qkm

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