6mo6

Crystal structure of the selenomethionine-substituted human sulfide:quinone oxidoreductase

spinqualitylabelsall models 6mo6, resolution 2.59Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6mo6 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 2.59Å Ligands: CL, CSS, FAD, MSE 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). 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Quinone reductase 3D structures 3D structures of sulfide quinone oxidoreductase

Proteopedia Page Contributors and Editors (what is this?)

OCA