3WRA

Crystal structure of the desB-Gallate complex exposed to Aerobic Atomosphere

3WRA の概要

• エントリーDOI: 10.2210/pdb3wra/pdb
• 関連するPDBエントリー: 3WKU 3WPM 3WR3 3WR4 3WR8 3WR9 3WRB 3WRC
• 分子名称: Gallate dioxygenase, FE (II) ION (3 entities in total)
• 機能のキーワード: oxidoreductase, extradiol dioxygenase, fe2+ binding, domain-swap dimer
• 由来する生物種: Sphingomonas paucimobilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 94018.02

構造登録者

Sugimoto, K.,Senda, M.,Kasai, D.,Fukuda, M.,Masai, E.,Senda, T. (登録日: 2014-02-21, 公開日: 2014-04-30, 最終更新日: 2024-04-03)

主引用文献

Sugimoto, K.,Senda, M.,Kasai, D.,Fukuda, M.,Masai, E.,Senda, T.
Molecular Mechanism of Strict Substrate Specificity of an Extradiol Dioxygenase, DesB, Derived from Sphingobium sp. SYK-6
Plos One, 9:e92249-e92249, 2014

PubMed Abstract: DesB, which is derived from Sphingobium sp. SYK-6, is a type II extradiol dioxygenase that catalyzes a ring opening reaction of gallate. While typical extradiol dioxygenases show broad substrate specificity, DesB has strict substrate specificity for gallate. The substrate specificity of DesB seems to be required for the efficient growth of S. sp. SYK-6 using lignin-derived aromatic compounds. Since direct coordination of hydroxyl groups of the substrate to the non-heme iron in the active site is a critical step for the catalytic reaction of the extradiol dioxygenases, the mechanism of the substrate recognition and coordination of DesB was analyzed by biochemical and crystallographic methods. Our study demonstrated that the direct coordination between the non-heme iron and hydroxyl groups of the substrate requires a large shift of the Fe (II) ion in the active site. Mutational analysis revealed that His124 and His192 in the active site are essential to the catalytic reaction of DesB. His124, which interacts with OH (4) of the bound gallate, seems to contribute to proper positioning of the substrate in the active site. His192, which is located close to OH (3) of the gallate, is likely to serve as the catalytic base. Glu377' interacts with OH (5) of the gallate and seems to play a critical role in the substrate specificity. Our biochemical and structural study showed the substrate recognition and catalytic mechanisms of DesB.

PubMed: 24657997
DOI: 10.1371/journal.pone.0092249

実験手法

X-RAY DIFFRACTION (2.1 Å)