5kli | pdb_00005kli

Rhodobacter sphaeroides bc1 with stigmatellin and antimycin

spinqualitylabelsall models 5kli, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5kli is a 12 chain structure with sequence from "rhodococcus_capsulatus"_molisch_1907 "rhodococcus capsulatus" molisch 1907. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ANJ, FES, HEC, HEM, LOP, SMA, SR Related: 5kkz, 5klv Gene: petB, fbcB ("Rhodococcus capsulatus" Molisch 1907), petC, fbcC ("Rhodococcus capsulatus" Molisch 1907), petA, fbcF ("Rhodococcus capsulatus" Molisch 1907) 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. [CY1_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. c1 functions as an electron donor to cytochrome c. Publication Abstract from PubMed The Complex III or cytochrome bc1 (cyt bc1) complex constitutes an integral part of the respiratory chain of most aerobic organisms and of the photosynthetic apparatus of anoxygenic purple bacteria. The function of cyt bc1 is to couple the reaction of electron transfer (ET) from ubiquinol to cytochrome c to proton pumping across the membrane. Mechanistically, the ET reaction requires docking of its Rieske iron-sulfur protein (ISP) subunit to the quinol oxidation (QP) site of the complex. Formation of an H-bond between the ISP and the bound substrate was proposed to mediate the docking. Here we show that the binding of oxazolidinedione-type inhibitors famoxadone, jg144, and fenamidone induces docking of the ISP to the QP site in the absence of the H-bond formation both in mitochondrial and bacterial cyt bc1 complexes, demonstrating that ISP docking is independent of the proposed H-bond. The binding of oxazolidinedione-type inhibitors to cyt bc1 of different species reveals a toxophore that appears to interact optimally with residues in the QP site. The effect of modifications or additions to the toxophore on the binding of cyt bc1 from different species could not be predicted from structure-based sequence alignment, as demonstrated by the altered binding mode of famoxadone to the bacterial cyt bc1. Hydrogen Bonding to the substrate is not required for Rieske iron-sulfur protein docking to the quinol oxidation site of complex III.,Esser L, Zhou F, Zhou Y, Xiao Y, Tang WK, Yu CA, Qin Z, Xia D J Biol Chem. 2016 Oct 7. pii: jbc.M116.744391. PMID:27758861 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome C 3D structures

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