2WDQ

E. coli succinate:quinone oxidoreductase (SQR) with carboxin bound

2WDQ の概要

• エントリーDOI: 10.2210/pdb2wdq/pdb
• 関連するPDBエントリー: 1NEK 1NEN 2ACZ 2WDR
• 分子名称: SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT, IRON/SULFUR CLUSTER, FE3-S4 CLUSTER, ... (14 entities in total)
• 機能のキーワード: succinate dehydrogenase activity, cell inner membrane, tricarboxylic acid cycle, cell membrane, metal-binding, transmembrane, transport, iron-sulfur, flavoprotein, oxidoreductase, electron transport, fad, iron, heme, membrane
• 由来する生物種: ESCHERICHIA COLI; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 363608.81

構造登録者

Ruprecht, J.,Yankovskaya, V.,Maklashina, E.,Iwata, S.,Cecchini, G. (登録日: 2009-03-25, 公開日: 2009-08-25, 最終更新日: 2024-10-23)

主引用文献

Ruprecht, J.,Yankovskaya, V.,Maklashina, E.,Iwata, S.,Cecchini, G.
Structure of Escherichia coli succinate:quinone oxidoreductase with an occupied and empty quinone-binding site.
J. Biol. Chem., 284:29836-29846, 2009

PubMed Abstract: Three new structures of Escherichia coli succinate-quinone oxidoreductase (SQR) have been solved. One with the specific quinone-binding site (Q-site) inhibitor carboxin present has been solved at 2.4 A resolution and reveals how carboxin inhibits the Q-site. The other new structures are with the Q-site inhibitor pentachlorophenol and with an empty Q-site. These structures reveal important details unresolved in earlier structures. Comparison of the new SQR structures shows how subtle rearrangements of the quinone-binding site accommodate the different inhibitors. The position of conserved water molecules near the quinone binding pocket leads to a reassessment of possible water-mediated proton uptake networks that complete reduction of ubiquinone. The dicarboxylate-binding site in the soluble domain of SQR is highly similar to that seen in high resolution structures of avian SQR (PDB 2H88) and soluble flavocytochrome c (PDB 1QJD) showing mechanistically significant structural features conserved across prokaryotic and eukaryotic SQRs.

PubMed: 19710024
DOI: 10.1074/jbc.M109.010058

実験手法

X-RAY DIFFRACTION (2.4 Å)