6AWF

Escherichia coli quinol:fumarate reductase crystallized without dicarboxylate

6AWF の概要

• エントリーDOI: 10.2210/pdb6awf/pdb
• 関連するPDBエントリー: 1KF6
• 分子名称: Fumarate reductase flavoprotein subunit, Fumarate reductase iron-sulfur subunit, Fumarate reductase subunit C, ... (9 entities in total)
• 機能のキーワード: complex ii, quinol:fumarate reductase, fumarate reductase, succinate dehydrogenase, succinate oxidase, succinate:quinone oxidoreductase, fad, flavoprotein, flavoenzyme, electron transport
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 245601.72

構造登録者

Iverson, T.M. (登録日: 2017-09-05, 公開日: 2017-12-06, 最終更新日: 2024-10-16)

主引用文献

Starbird, C.A.,Tomasiak, T.M.,Singh, P.K.,Yankovskaya, V.,Maklashina, E.,Eisenbach, M.,Cecchini, G.,Iverson, T.M.
New crystal forms of the integral membrane Escherichia coli quinol:fumarate reductase suggest that ligands control domain movement.
J. Struct. Biol., 202:100-104, 2018

PubMed Abstract: Quinol:fumarate reductase (QFR) is an integral membrane protein and a member of the respiratory Complex II superfamily. Although the structure of Escherichia coli QFR was first reported almost twenty years ago, many open questions of catalysis remain. Here we report two new crystal forms of QFR, one grown from the lipidic cubic phase and one grown from dodecyl maltoside micelles. QFR crystals grown from the lipid cubic phase processed as P1, merged to 7.5 Å resolution, and exhibited crystal packing similar to previous crystal forms. Crystals grown from dodecyl maltoside micelles processed as P2, merged to 3.35 Å resolution, and displayed a unique crystal packing. This latter crystal form provides the first view of the E. coli QFR active site without a dicarboxylate ligand. Instead, an unidentified anion binds at a shifted position. In one of the molecules in the asymmetric unit, this is accompanied by rotation of the capping domain of the catalytic subunit. In the other molecule, this is associated with loss of interpretable electron density for this same capping domain. Analysis of the structure suggests that the ligand adjusts the position of the capping domain.

PubMed: 29158068
DOI: 10.1016/j.jsb.2017.11.004

実験手法

X-RAY DIFFRACTION (3.35 Å)