6mp5

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of native human sulfide:quinone oxidoreductase

Structural highlights

6mp5 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.99Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[1]

Publication Abstract from PubMed

Hydrogen 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.

References

↑ Jackson MR, Melideo SL, Jorns MS. Human sulfide:quinone oxidoreductase catalyzes the first step in hydrogen sulfide metabolism and produces a sulfane sulfur metabolite. Biochemistry. 2012 Aug 28;51(34):6804-15. doi: 10.1021/bi300778t. Epub 2012 Aug, 20. PMID:22852582 doi:http://dx.doi.org/10.1021/bi300778t
↑ Jackson MR, Loll PJ, Jorns MS. X-Ray Structure of Human Sulfide:Quinone Oxidoreductase: Insights into the Mechanism of Mitochondrial Hydrogen Sulfide Oxidation. Structure. 2019 Mar 15. pii: S0969-2126(19)30080-2. doi:, 10.1016/j.str.2019.03.002. PMID:30905673 doi:http://dx.doi.org/10.1016/j.str.2019.03.002

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6mp5"

Categories: Homo sapiens | Large Structures | Jackson MR | Jorns MS | Loll PJ

@@ Line 3: / Line 3: @@
 <StructureSection load='6mp5' size='340' side='right'caption='[[6mp5]], [[Resolution|resolution]] 2.99&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6mp5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MP5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MP5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6mp5]] 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=6MP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MP5 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.99&#8491;</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></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SQOR, SQRDL, CGI-44 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6mp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mp5 OCA], [https://pdbe.org/6mp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mp5 RCSB], [https://www.ebi.ac.uk/pdbsum/6mp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mp5 ProSAT]</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=6mp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mp5 OCA], [http://pdbe.org/6mp5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mp5 RCSB], [http://www.ebi.ac.uk/pdbsum/6mp5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mp5 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[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 ==
@@ Line 20: / Line 19: @@
 </div>
 <div class="pdbe-citations 6mp5" 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/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Jackson, M R]]
+[[Category: Jackson MR]]
-[[Category: Jorns, M S]]
+[[Category: Jorns MS]]
-[[Category: Loll, P J]]
+[[Category: Loll PJ]]
-[[Category: Hydrogen sulfide metabolism]]
-[[Category: Membrane protein]]
-[[Category: Oxidoreductase]]
-[[Category: Rossmann fold]]
-[[Category: Sulfide:quinone oxidoreductase]]
-[[Category: Thiocystine]]

6mp5

From Proteopedia

Current revision

Crystal structure of native human sulfide:quinone oxidoreductase

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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