6mo6: Difference between revisions
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<StructureSection load='6mo6' size='340' side='right'caption='[[6mo6]], [[Resolution|resolution]] 2.59Å' scene=''> | <StructureSection load='6mo6' size='340' side='right'caption='[[6mo6]], [[Resolution|resolution]] 2.59Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6mo6]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6mo6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MO6 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.59Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=6mo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mo6 OCA], [https://pdbe.org/6mo6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mo6 RCSB], [https://www.ebi.ac.uk/pdbsum/6mo6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mo6 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/SQOR_HUMAN SQOR_HUMAN] Catalyzes the oxidation of hydrogen sulfide with the help of a quinone, such as ubiquinone, giving rise to thiosulfate and ultimately to sulfane (molecular sulfur) atoms. Requires an additional electron acceptor; can use sulfite, sulfide or cyanide (in vitro).<ref>PMID:22852582</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6mo6" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6mo6" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Quinone reductase 3D structures|Quinone reductase 3D structures]] | |||
*[[3D structures of sulfide quinone oxidoreductase|3D structures of sulfide quinone oxidoreductase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Jackson | [[Category: Jackson MR]] | ||
[[Category: Jorns | [[Category: Jorns MS]] | ||
[[Category: Loll | [[Category: Loll PJ]] | ||
Latest revision as of 15:52, 6 November 2024
Crystal structure of the selenomethionine-substituted human sulfide:quinone oxidoreductaseCrystal structure of the selenomethionine-substituted human sulfide:quinone oxidoreductase
Structural highlights
FunctionSQOR_HUMAN Catalyzes the oxidation of hydrogen sulfide with the help of a quinone, such as ubiquinone, giving rise to thiosulfate and ultimately to sulfane (molecular sulfur) atoms. Requires an additional electron acceptor; can use sulfite, sulfide or cyanide (in vitro).[1] Publication Abstract from PubMedHydrogen sulfide (H2S) is a gasotransmitter exhibiting pivotal functions in diverse biological processes, including activation of multiple cardioprotective pathways. Sulfide:quinone oxidoreductase (SQOR) is an integral membrane flavoprotein that catalyzes the first step in the mitochondrial metabolism of H2S. As such, it plays a critical role in controlling physiological levels of the gasotransmitter and has attracted keen interest as a potential drug target. We report the crystal structure of human SQOR, unraveling the molecular basis for the enzyme's ability to catalyze sulfane sulfur transfer reactions with structurally diverse acceptors. We demonstrate that human SQOR contains unique features: an electropositive surface depression implicated as a binding site for sulfane sulfur acceptors and postulated to funnel negatively charged substrates to a hydrophilic H2S-oxidizing active site, which is connected to a hydrophobic internal tunnel that binds coenzyme Q. These findings support a proposed model for catalysis and open the door for structure-based drug design. X-Ray Structure of Human Sulfide:Quinone Oxidoreductase: Insights into the Mechanism of Mitochondrial Hydrogen Sulfide Oxidation.,Jackson MR, Loll PJ, Jorns MS Structure. 2019 Mar 15. pii: S0969-2126(19)30080-2. doi:, 10.1016/j.str.2019.03.002. PMID:30905673[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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