5KLV
Structure of bos taurus cytochrome bc1 with fenamidone inhibited
Summary for 5KLV
| Entry DOI | 10.2210/pdb5klv/pdb |
| Related | 5KKZ 5KLI |
| Descriptor | Cytochrome b-c1 complex subunit 1, mitochondrial, Cytochrome b-c1 complex subunit 9, Cytochrome b-c1 complex subunit 10, ... (23 entities in total) |
| Functional Keywords | mitochondrial respiratory chain, cytochrome bc1 complex, fenamidone, electron transfer, oxidoreductase |
| Biological source | Bos taurus (Bovine) More |
| Cellular location | Mitochondrion inner membrane; Peripheral membrane protein; Matrix side: P31800 P23004 Mitochondrion inner membrane: P00130 P07552 P00129 P13271 P00126 Mitochondrion inner membrane ; Multi-pass membrane protein : P00157 Mitochondrion inner membrane; Single-pass membrane protein; Intermembrane side: P00125 Mitochondrion inner membrane; Single-pass membrane protein: P13272 P13272 |
| Total number of polymer chains | 11 |
| Total formula weight | 251059.43 |
| Authors | |
| Primary citation | Esser, L.,Zhou, F.,Zhou, Y.,Xiao, Y.,Tang, W.K.,Yu, C.A.,Qin, Z.,Xia, D. Hydrogen Bonding to the Substrate Is Not Required for Rieske Iron-Sulfur Protein Docking to the Quinol Oxidation Site of Complex III. J.Biol.Chem., 291:25019-25031, 2016 Cited by PubMed Abstract: Complex III or the cytochrome (cyt) bc 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 bc is to couple the reaction of electron transfer from ubiquinol to cytochrome c to proton pumping across the membrane. Mechanistically, the electron transfer reaction requires docking of its Rieske iron-sulfur protein (ISP) subunit to the quinol oxidation site (Q) 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 Q site in the absence of the H-bond formation both in mitochondrial and bacterial cyt bc complexes, demonstrating that ISP docking is independent of the proposed direct ISP-inhibitor interaction. The binding of oxazolidinedione-type inhibitors to cyt bc of different species reveals a toxophore that appears to interact optimally with residues in the Q site. The effect of modifications or additions to the toxophore on the binding to cyt bc from different species could not be predicted from structure-based sequence alignments, as demonstrated by the altered binding mode of famoxadone to bacterial cyt bc. PubMed: 27758861DOI: 10.1074/jbc.M116.744391 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.652 Å) |
Structure validation
Download full validation report
