2qjp | pdb_00002qjp

Crystal structure of wild type rhodobacter sphaeroides with stigmatellin and antimycin inhibited

spinqualitylabelsall models 2qjp, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2qjp is a 12 chain structure with sequence from "luteovulum_sphaeroides"_(van_niel_1944)_suresh_et_al._2019 "luteovulum sphaeroides" (van niel 1944) suresh et al. 2019. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ANJ, BGL, FES, HEM, LOP, SMA, SR Related: 2qjk, 1zrt, 1kb9, 1ntk, 1sqx, 1l0n Gene: petB, fbcB ("Luteovulum sphaeroides" (van Niel 1944) Suresh et al. 2019), fbcC ("Luteovulum sphaeroides" (van Niel 1944) Suresh et al. 2019), petA, fbcF ("Luteovulum sphaeroides" (van Niel 1944) Suresh et al. 2019) Activity: Ubiquinol--cytochrome-c reductase, with EC number 1.10.2.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CYB_RHOSH] 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_RHOSH] 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. 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 cytochrome bc(1) complex (bc(1)) is a major contributor to the proton motive force across the membrane by coupling electron transfer to proton translocation. The crystal structures of wild type and mutant bc(1) complexes from the photosynthetic purple bacterium Rhodobacter sphaeroides (Rsbc(1)), stabilized with the quinol oxidation (Q(P)) site inhibitor stigmatellin alone or in combination with the quinone reduction (Q(N)) site inhibitor antimycin, were determined. The high quality electron density permitted assignments of a new metal-binding site to the cytochrome c(1) subunit and a number of lipid and detergent molecules. Structural differences between Rsbc(1) and its mitochondrial counterparts are mostly extra membranous and provide a basis for understanding the function of the predominantly longer sequences in the bacterial subunits. Functional implications for the bc(1) complex are derived from analyses of 10 independent molecules in various crystal forms and from comparisons with mitochondrial complexes. Inhibitor-complexed structures of the cytochrome bc1 from the photosynthetic bacterium Rhodobacter sphaeroides.,Esser L, Elberry M, Zhou F, Yu CA, Yu L, Xia D J Biol Chem. 2008 Feb 1;283(5):2846-57. Epub 2007 Nov 26. PMID:18039651 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome C 3D structures Cytochrome bc1 complex

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