1D6Y

CRYSTAL STRUCTURE OF E. COLI COPPER-CONTAINING AMINE OXIDASE ANAEROBICALLY REDUCED WITH BETA-PHENYLETHYLAMINE AND COMPLEXED WITH NITRIC OXIDE.

1D6Y の概要

• エントリーDOI: 10.2210/pdb1d6y/pdb
• 関連するPDBエントリー: 1d6u 1d6y 1d6z 1jez 1oac 1qaf 1qak 1qal 1spu
• 分子名称: COPPER AMINE OXIDASE, COPPER (II) ION, CALCIUM ION, ... (8 entities in total)
• 機能のキーワード: reaction intermediate mimic, oxidoreductase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm: P46883
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 163629.61

構造登録者

Wilmot, C.M.,Hajdu, J.,McPherson, M.J.,Knowles, P.F.,Phillips, S.E.V. (登録日: 1999-10-16, 公開日: 2000-02-02, 最終更新日: 2024-11-06)

主引用文献

Wilmot, C.M.,Hajdu, J.,McPherson, M.J.,Knowles, P.F.,Phillips, S.E.
Visualization of dioxygen bound to copper during enzyme catalysis.
Science, 286:1724-1728, 1999

PubMed Abstract: X-ray crystal structures of three species related to the oxidative half of the reaction of the copper-containing quinoprotein amine oxidase from Escherichia coli have been determined. Crystals were freeze-trapped either anaerobically or aerobically after exposure to substrate, and structures were determined to resolutions between 2.1 and 2.4 angstroms. The oxidation state of the quinone cofactor was investigated by single-crystal spectrophotometry. The structures reveal the site of bound dioxygen and the proton transfer pathways involved in oxygen reduction. The quinone cofactor is regenerated from the iminoquinone intermediate by hydrolysis involving Asp383, the catalytic base in the reductive half-reaction. Product aldehyde inhibits the hydrolysis, making release of product the rate-determining step of the reaction in the crystal.

PubMed: 10576737
DOI: 10.1126/science.286.5445.1724

実験手法

X-RAY DIFFRACTION (2.4 Å)