1L0N

native structure of bovine mitochondrial cytochrome bc1 complex

1L0N の概要

• エントリーDOI: 10.2210/pdb1l0n/pdb
• 分子名称: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I, Ubiquinol-cytochrome C reductase complex 7.2 kDa protein, cytochrome b-c1 complex 6.4K protein, ... (13 entities in total)
• 機能のキーワード: cytochrome bc1, membrane protein, heme protein, iron sulfur protein, cytochrome b, cytochrome c1, mitochondrial processing protease, mpp, oxidoreductase
• 由来する生物種: Bos taurus (cattle); 詳細
• 細胞内の位置: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side: P31800 P23004; Mitochondrion inner membrane: P00130 P07552 P13272 P00129 P13271 P00126 P13272; Mitochondrion inner membrane; Multi-pass membrane protein (By similarity): P00157; Mitochondrion inner membrane; Single-pass membrane protein; Intermembrane side: P00125
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 243099.42

構造登録者

Gao, X.,Wen, X.,Yu, C.A.,Esser, L.,Tsao, S.,Quinn, B.,Zhang, L.,Yu, L.,Xia, D. (登録日: 2002-02-11, 公開日: 2003-04-08, 最終更新日: 2024-10-09)

主引用文献

Gao, X.,Wen, X.,Yu, C.A.,Esser, L.,Tsao, S.,Quinn, B.,Zhang, L.,Yu, L.,Xia, D.
The Crystal Structure of Mitochondrial Cytochrome bc1 in Complex with Famoxadone: The Role of Aromatic-Aromatic Interaction in Inhibition
Biochemistry, 41:11692-11702, 2003

PubMed Abstract: Ubiquinol cytochrome c oxido-reductase (EC. 1.10.2.2, bc1) is an integral membrane protein complex essential to cellular respiration. Structures of the 11-subunit mitochondrial bc1 complex were determined with and without the fungicide famoxadone. Specific inhibition by famoxadone is achieved through a coordinated optimization of aromatic-aromatic interactions where conformational rearrangements in famoxadone and in residues lining the inhibitor-binding pocket produce a network of aromatic-aromatic interactions that mimic the crystal lattice of benzene. The profound aromatic-aromatic interactions as supported by prior mutagenesis provide a structural basis for specific protein-ligand interaction in a hydrophobic environment. Dramatic conformational changes, both in cyt. b and ISP subunits in the inhibitor-protein complex, confer experimental evidence for a functional role of cytochrome b in the induced conformational arrest of ISP and allow the identification of a possible intrasubunit signal transduction pathway that controls the movement of ISP. These results support an inhibitory mechanism that is consistent with the requirement for ISP movement in the electron transfer of this complex.

PubMed: 12269811
DOI: 10.1021/bi026252p

実験手法

X-RAY DIFFRACTION (2.6 Å)