4N2X

Crystal Structure of DL-2-haloacid dehalogenase

4N2X の概要

• エントリーDOI: 10.2210/pdb4n2x/pdb
• 分子名称: DL-2-haloacid dehalogenase, GLYCEROL (3 entities in total)
• 機能のキーワード: dehalogenases, hydrolase
• 由来する生物種: Methylobacterium
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 205530.24

構造登録者

Siwek, A.,Omi, R.,Hirotsu, K.,Jitsumori, K.,Esaki, N.,Kurihara, T.,Paneth, P. (登録日: 2013-10-06, 公開日: 2013-11-27, 最終更新日: 2024-03-20)

主引用文献

Siwek, A.,Omi, R.,Hirotsu, K.,Jitsumori, K.,Esaki, N.,Kurihara, T.,Paneth, P.
Binding modes of DL-2-haloacid dehalogenase revealed by crystallography, modeling and isotope effects studies.
Arch.Biochem.Biophys., 540:26-32, 2013

PubMed Abstract: Several pathways of biotic dechlorination can be found in enzymes, each characterized by different chlorine isotopic fractionation, which can thus serve as a signature of a particular mechanism. Unlike other dehalogenases, DL-2-haloacid dehalogenase, DL-DEX, converts both enantiomers of the substrate. Chlorine isotope effects for this enzyme are larger than in the case of other dehalogenases. Recently, the 3D structure of this enzyme became available and enabled us to model these isotope effects and seek their origin. We show that the elevated values of the chlorine kinetic isotope effects originate in part in the processes of binding and migration within the enzyme active site that precede the dehalogenation step.

PubMed: 24071515
DOI: 10.1016/j.abb.2013.09.012

実験手法

X-RAY DIFFRACTION (1.7 Å)