5KLV

Structure of bos taurus cytochrome bc1 with fenamidone inhibited

5KLV の概要

• エントリーDOI: 10.2210/pdb5klv/pdb
• 関連するPDBエントリー: 5KKZ 5KLI
• 分子名称: Cytochrome b-c1 complex subunit 1, mitochondrial, Cytochrome b-c1 complex subunit 9, Cytochrome b-c1 complex subunit 10, ... (23 entities in total)
• 機能のキーワード: mitochondrial respiratory chain, cytochrome bc1 complex, fenamidone, electron transfer, oxidoreductase
• 由来する生物種: Bos taurus (Bovine); 詳細
• 細胞内の位置: 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
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 251059.43

構造登録者

Xia, D.,Esser, L.,Zhou, F.,Zhou, Y.,Xiao, Y.,Tang, W.K.,Yu, C.A.,Qin, Z. (登録日: 2016-06-25, 公開日: 2016-10-12, 最終更新日: 2024-10-30)

主引用文献

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

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: 27758861
DOI: 10.1074/jbc.M116.744391

実験手法

X-RAY DIFFRACTION (2.652 Å)