6oi5: Difference between revisions
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==Crystal structure of human Sulfide Quinone Oxidoreductase== | |||
<StructureSection load='6oi5' size='340' side='right'caption='[[6oi5]], [[Resolution|resolution]] 2.81Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6oi5]] is a 2 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=6OI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OI5 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]] 2.811Å</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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=6oi5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oi5 OCA], [https://pdbe.org/6oi5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oi5 RCSB], [https://www.ebi.ac.uk/pdbsum/6oi5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oi5 ProSAT]</span></td></tr> | |||
</table> | |||
== 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;"> | |||
== Publication Abstract from PubMed == | |||
Mitochondrial sulfide quinone oxidoreductase (SQR) catalyzes the oxidation of H2S to glutathione persulfide with concomitant reduction of CoQ10. We report herein that the promiscuous activity of human SQR supported the conversion of CoA to CoA-SSH (CoA-persulfide), a potent inhibitor of butyryl-CoA dehydrogenase, and revealed a molecular link between sulfide and butyrate metabolism, which are known to interact. Three different CoQ1-bound crystal structures furnished insights into how diverse substrates access human SQR, and provided snapshots of the reaction coordinate. Unexpectedly, the active site cysteines in SQR are configured in a bridging trisulfide at the start and end of the catalytic cycle, and the presence of sulfane sulfur was confirmed biochemically. Importantly, our study leads to a mechanistic proposal for human SQR in which sulfide addition to the trisulfide cofactor eliminates (201)Cys-SSH, forming an intense charge-transfer complex with flavin adenine dinucleotide, and (379)Cys-SSH, which transfers sulfur to an external acceptor. | |||
A Catalytic Trisulfide in Human Sulfide Quinone Oxidoreductase Catalyzes Coenzyme A Persulfide Synthesis and Inhibits Butyrate Oxidation.,Landry AP, Moon S, Kim H, Yadav PK, Guha A, Cho US, Banerjee R Cell Chem Biol. 2019 Nov 21;26(11):1515-1525.e4. doi:, 10.1016/j.chembiol.2019.09.010. Epub 2019 Oct 4. PMID:31591036<ref>PMID:31591036</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6oi5" style="background-color:#fffaf0;"></div> | ||
[[Category: Cho | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Quinone reductase 3D structures|Quinone reductase 3D structures]] | ||
*[[Sulfide quinone oxidoreductase|Sulfide quinone oxidoreductase]] | |||
*[[3D structures of sulfide quinone oxidoreductase|3D structures of sulfide quinone oxidoreductase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Banerjee R]] | |||
[[Category: Cho US]] | |||
[[Category: Kim H]] | |||
[[Category: Moon S]] | |||
Latest revision as of 14:15, 30 October 2024
Crystal structure of human Sulfide Quinone OxidoreductaseCrystal structure of 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 PubMedMitochondrial sulfide quinone oxidoreductase (SQR) catalyzes the oxidation of H2S to glutathione persulfide with concomitant reduction of CoQ10. We report herein that the promiscuous activity of human SQR supported the conversion of CoA to CoA-SSH (CoA-persulfide), a potent inhibitor of butyryl-CoA dehydrogenase, and revealed a molecular link between sulfide and butyrate metabolism, which are known to interact. Three different CoQ1-bound crystal structures furnished insights into how diverse substrates access human SQR, and provided snapshots of the reaction coordinate. Unexpectedly, the active site cysteines in SQR are configured in a bridging trisulfide at the start and end of the catalytic cycle, and the presence of sulfane sulfur was confirmed biochemically. Importantly, our study leads to a mechanistic proposal for human SQR in which sulfide addition to the trisulfide cofactor eliminates (201)Cys-SSH, forming an intense charge-transfer complex with flavin adenine dinucleotide, and (379)Cys-SSH, which transfers sulfur to an external acceptor. A Catalytic Trisulfide in Human Sulfide Quinone Oxidoreductase Catalyzes Coenzyme A Persulfide Synthesis and Inhibits Butyrate Oxidation.,Landry AP, Moon S, Kim H, Yadav PK, Guha A, Cho US, Banerjee R Cell Chem Biol. 2019 Nov 21;26(11):1515-1525.e4. doi:, 10.1016/j.chembiol.2019.09.010. Epub 2019 Oct 4. PMID:31591036[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also
References
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