2QJK

Crystal Structure Analysis of mutant rhodobacter sphaeroides bc1 with stigmatellin and antimycin

2QJK の概要

• エントリーDOI: 10.2210/pdb2qjk/pdb
• 関連するPDBエントリー: 1KB9 1NTK 1ZRT 2FYN 2QJP
• 分子名称: Cytochrome b, FE2/S2 (INORGANIC) CLUSTER, Cytochrome c1, ... (10 entities in total)
• 機能のキーワード: cytochrome b, tm helices, cytochrome c1, c-terminal tm helix, iron-sulfur-protein, n-terminal tm, electron transport, heme, membrane, metal-binding, respiratory chain, transmembrane, transport, 2fe-2s, inner membrane, oxidoreductase
• 由来する生物種: Rhodobacter sphaeroides; 詳細
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 596482.06

構造登録者

Esser, L. (登録日: 2007-07-07, 公開日: 2007-12-25, 最終更新日: 2024-10-16)

主引用文献

Esser, L.,Elberry, M.,Zhou, F.,Yu, C.A.,Yu, L.,Xia, D.
Inhibitor-complexed structures of the cytochrome bc1 from the photosynthetic bacterium Rhodobacter sphaeroides.
J.Biol.Chem., 283:2846-2857, 2008

PubMed Abstract: 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.

PubMed: 18039651
DOI: 10.1074/jbc.M708608200

実験手法

X-RAY DIFFRACTION (3.1 Å)