3A18

Crystal Structure of Aldoxime Dehydratase (OxdRE) in Complex with Butyraldoxime (soaked crystal)

3A18 の概要

• エントリーDOI: 10.2210/pdb3a18/pdb
• 関連するPDBエントリー: 3A15 3A16 3A17
• 分子名称: Aldoxime dehydratase, PROTOPORPHYRIN IX CONTAINING FE, (1Z)-butanal oxime, ... (4 entities in total)
• 機能のキーワード: beta barrel, heme protein, lyase
• 由来する生物種: Rhodococcus erythropolis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 171144.93

構造登録者

Sawai, H.,Sugimoto, H.,Kato, Y.,Asano, Y.,Shiro, Y.,Aono, S. (登録日: 2009-03-26, 公開日: 2009-09-08, 最終更新日: 2023-11-01)

主引用文献

Sawai, H.,Sugimoto, H.,Kato, Y.,Asano, Y.,Shiro, Y.,Aono, S.
X-ray crystal structure of michaelis complex of aldoxime dehydratase
J.Biol.Chem., 284:32089-32096, 2009

PubMed Abstract: Aldoxime dehydratase (Oxd) catalyzes the dehydration of aldoximes (R-CH=N-OH) to their corresponding nitrile (R-C triple bond N). Oxd is a heme-containing enzyme that catalyzes the dehydration reaction as its physiological function. We have determined the first two structures of Oxd: the substrate-free OxdRE at 1.8 A resolution and the n-butyraldoxime- and propionaldoxime-bound OxdREs at 1.8 and 1.6 A resolutions, respectively. Unlike other heme enzymes, the organic substrate is directly bound to the heme iron in OxdRE. We determined the structure of the Michaelis complex of OxdRE by using the unique substrate binding and activity regulation properties of Oxd. The Michaelis complex was prepared by x-ray cryoradiolytic reduction of the ferric dead-end complex in which Oxd contains a Fe(3+) heme form. The crystal structures reveal the mechanism of substrate recognition and the catalysis of OxdRE.

PubMed: 19740758
DOI: 10.1074/jbc.M109.018762

実験手法

X-RAY DIFFRACTION (1.8 Å)