3h1k

Chicken cytochrome BC1 complex with ZN++ and an iodinated derivative of kresoxim-methyl bound

spinqualitylabelsall models 3h1k, resolution 3.48Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3h1k is a 20 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BOG, CDL, FES, GOL, HEC, HEM, IKR, PEE, UNL, UQ, ZN NonStd Res: UNK Related: 1bbc, 2ppj, 3cx5, 2fyu Activity: Ubiquinol--cytochrome-c reductase, with EC number 1.10.2.2 Resources: FirstGlance, OCA, RCSB, PDBsum Function [CYB_CHICK] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis (By similarity). [UCRI_CHICK] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The chicken mitochondrial ubiquinol cytochrome c oxidoreductase (bc(1) complex) is inhibited by Zn(2+) ions, but with higher K(i) ( approximately 3 microM) than the corresponding bovine enzyme. When equilibrated with mother liquor containing 200 microM ZnCl(2) for 7 days, the crystalline chicken bc(1) complex specifically binds Zn(2+) at 4 sites representing two sites on each monomer in the dimer. These two sites are close to the stigmatellin-binding site, taken to be center Q(o) of the Q-cycle mechanism, and are candidates for the inhibitory site. One binding site is actually in the hydrophobic channel between the Q(o) site and the bulk lipid phase, and may interfere with quinone binding. The other is in a hydrophilic area between cytochromes b and c(1), and might interfere with the egress of protons from the Q(o) site to the intermembrane aqueous medium. No zinc was bound near the putative proteolytic active site of subunits 1 and 2 (homologous to mitochondrial processing peptidase) under these conditions. Crystallographic location of two Zn(2+)-binding sites in the avian cytochrome bc(1) complex.,Berry EA, Zhang Z, Bellamy HD, Huang L Biochim Biophys Acta. 2000 Aug 15;1459(2-3):440-8. PMID:11004461 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome bc1 complex

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