3EJ9

Structural and mechanistic analysis of trans-3-chloroacrylic acid dehalogenase activity

3EJ9 の概要

• エントリーDOI: 10.2210/pdb3ej9/pdb
• 関連するPDBエントリー: 3EJ3 3EJ7
• 分子名称: Alpha-subunit of trans-3-chloroacrylic acid dehalogenase, Beta-subunit of trans-3-chloroacrylic acid dehalogenase (3 entities in total)
• 機能のキーワード: trans-3-chloroacrylic acid dehalogenase, caad, dehalogenase, isomerase, hydrolase
• 由来する生物種: Pseudomonas pavonaceae; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 48006.86

構造登録者

Pegan, S.,Serrano, H.,Whitman, C.P.,Mesecar, A.D. (登録日: 2008-09-17, 公開日: 2008-12-02, 最終更新日: 2023-08-30)

主引用文献

Pegan, S.D.,Serrano, H.,Whitman, C.P.,Mesecar, A.D.
Structural and mechanistic analysis of trans-3-chloroacrylic acid dehalogenase activity.
Acta Crystallogr.,Sect.D, 64:1277-1282, 2008

PubMed Abstract: Trans-3-chloroacrylic acid dehalogenase (CaaD) is a critical enzyme in the trans-1,3-dichloropropene (DCP) degradation pathway in Pseudomonas pavonaceae 170. This enzyme allows bacteria to use trans-DCP, a common component in commercially produced fumigants, as a carbon source. CaaD specifically catalyzes the fourth step of the pathway by cofactor-independent dehalogenation of a vinyl carbon-halogen bond. Previous studies have reported an X-ray structure of CaaD under acidic conditions with a covalent modification of the catalytic betaPro1 residue. Here, the 1.7 A resolution X-ray structure of CaaD under neutral (pH 6.5) conditions is reported without the presence of the covalent adduct. In this new structure, a substrate-like acetate molecule is bound within the active site in a position analogous to the putative substrate-binding site. Additionally, a catalytically important water molecule was identified, consistent with previously proposed reaction schemes. Finally, flexibility of the catalytically relevant side chain alphaGlu52 is observed in the structure, supporting its role in the catalytic mechanism.

PubMed: 19018104
DOI: 10.1107/S0907444908034707

実験手法

X-RAY DIFFRACTION (1.5 Å)