2WL3

crystal structure of catechol 2,3-dioxygenase

2WL3 の概要

• エントリーDOI: 10.2210/pdb2wl3/pdb
• 関連するPDBエントリー: 2WL9
• 分子名称: CATECHOL 2,3-DIOXYGENASE, FE (III) ION, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: aromatic hydrocarbons catabolism, akbc, oxidoreductase
• 由来する生物種: RHODOCOCCUS SP. DK17
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 138497.27

構造登録者

Cho, H.J.,Kim, K.J.,Kang, B.S. (登録日: 2009-06-21, 公開日: 2010-09-01, 最終更新日: 2024-11-06)

主引用文献

Cho, H.J.,Kim, K.,Sohn, S.Y.,Cho, H.Y.,Kim, K.J.,Kim, M.H.,Kim, D.,Kim, E.,Kang, B.S.
Substrate-Binding Mechanism of a Type I Extradiol Dioxygenase.
J.Biol.Chem., 285:34643-, 2010

PubMed Abstract: A meta-cleavage pathway for the aerobic degradation of aromatic hydrocarbons is catalyzed by extradiol dioxygenases via a two-step mechanism: catechol substrate binding and dioxygen incorporation. The binding of substrate triggers the release of water, thereby opening a coordination site for molecular oxygen. The crystal structures of AkbC, a type I extradiol dioxygenase, and the enzyme substrate (3-methylcatechol) complex revealed the substrate binding process of extradiol dioxygenase. AkbC is composed of an N-domain and an active C-domain, which contains iron coordinated by a 2-His-1-carboxylate facial triad motif. The C-domain includes a β-hairpin structure and a C-terminal tail. In substrate-bound AkbC, 3-methylcatechol interacts with the iron via a single hydroxyl group, which represents an intermediate stage in the substrate binding process. Structure-based mutagenesis revealed that the C-terminal tail and β-hairpin form part of the substrate binding pocket that is responsible for substrate specificity by blocking substrate entry. Once a substrate enters the active site, these structural elements also play a role in the correct positioning of the substrate. Based on the results presented here, a putative substrate binding mechanism is proposed.

PubMed: 20810655
DOI: 10.1074/JBC.M110.130310

実験手法

X-RAY DIFFRACTION (2.2 Å)