1T3Q

Crystal structure of quinoline 2-Oxidoreductase from Pseudomonas Putida 86

1T3Q の概要

• エントリーDOI: 10.2210/pdb1t3q/pdb
• 分子名称: quinoline 2-oxidoreductase small subunit, quinoline 2-oxidoreductase large subunit, quinoline 2-oxidoreductase medium subunit, ... (10 entities in total)
• 機能のキーワード: qor, molybdenum, mcd, oxidoreductase
• 由来する生物種: Pseudomonas putida; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 271598.31

構造登録者

Bonin, I.,Martins, B.M.,Purvanov, V.,Fetzner, S.,Huber, R.,Dobbek, H. (登録日: 2004-04-27, 公開日: 2004-09-14, 最終更新日: 2023-08-23)

主引用文献

Bonin, I.,Martins, B.M.,Purvanov, V.,Fetzner, S.,Huber, R.,Dobbek, H.
Active site geometry and substrate recognition of the molybdenum hydroxylase quinoline 2-oxidoreductase.
STRUCTURE, 12:1425-1435, 2004

PubMed Abstract: The soil bacterium Pseudomonas putida 86 uses quinoline as a sole source of carbon and energy. Quinoline 2-oxidoreductase (Qor) catalyzes the first metabolic step converting quinoline to 2-oxo-1,2-dihydroquinoline. Qor is a member of the molybdenum hydroxylases. The molybdenum ion is coordinated by two ene-dithiolate sulfur atoms, two oxo-ligands, and a catalytically crucial sulfido-ligand, whose position in the active site was controversial. The 1.8 A resolution crystal structure of Qor indicates that the sulfido-ligand occupies the equatorial position at the molybdenum ion. The structural comparison of Qor with the allopurinol-inhibited xanthine dehydrogenase from Rhodobacter capsulatus allows direct insight into the mechanism of substrate recognition and the identification of putative catalytic residues. The active site protein variants QorE743V and QorE743D were analyzed to assess the catalytic role of E743.

PubMed: 15296736
DOI: 10.1016/j.str.2004.05.014

実験手法

X-RAY DIFFRACTION (1.8 Å)