2E77

Crystal structure of L-lactate oxidase with pyruvate complex

2E77 の概要

• エントリーDOI: 10.2210/pdb2e77/pdb
• 関連するPDBエントリー: 2DU2
• 分子名称: Lactate oxidase, FLAVIN MONONUCLEOTIDE, PYRUVIC ACID, ... (4 entities in total)
• 機能のキーワード: tim barrel, fmn, oxidoreductase
• 由来する生物種: Aerococcus viridans
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 166012.97

構造登録者

Morimoto, Y. (登録日: 2007-01-06, 公開日: 2007-11-27, 最終更新日: 2023-11-15)

主引用文献

Li, S.J.,Umena, Y.,Yorita, K.,Matsuoka, T.,Kita, A.,Fukui, K.,Morimoto, Y.
Crystallographic study on the interaction of L-lactate oxidase with pyruvate at 1.9 Angstrom resolution.
Biochem.Biophys.Res.Commun., 358:1002-1007, 2007

PubMed Abstract: L-Lactate oxidase (LOX) from Aerococcus viridans catalyzes the oxidation of L-lactate to pyruvate by the molecular oxygen and belongs to a large family of 2-hydroxy acid-dependent flavoenzymes. To investigate the interaction of LOX with pyruvate in structural details and understand the chemical mechanism of flavin-dependent L-lactate dehydrogenation, the LOX-pyruvate complex was crystallized and the crystal structure of the complex has been solved at a resolution of 1.90 Angstrom. One pyruvate molecule bound to the active site and located near N5 position of FMN for subunits, A, B, and D in the asymmetric unit, were identified. The pyruvate molecule is stabilized by the interaction of its carboxylate group with the side-chain atoms of Tyr40, Arg181, His265, and Arg268, and of its keto-oxygen atom with the side-chain atoms of Tyr146, Tyr215, and His265. The alpha-carbon of pyruvate is found to be 3.13 Angstrom from the N5 atom of FMN at an angle of 105.4 degrees from the flavin N5-N10 axis.

PubMed: 17517371
DOI: 10.1016/j.bbrc.2007.05.021

実験手法

X-RAY DIFFRACTION (1.9 Å)