2W11

Structure of the L-2-haloacid dehalogenase from Sulfolobus tokodaii

2W11 の概要

• エントリーDOI: 10.2210/pdb2w11/pdb
• 関連するPDBエントリー: 2W43
• 分子名称: 2-HALOALKANOIC ACID DEHALOGENASE, (2S)-2-HYDROXYPROPANOIC ACID (3 entities in total)
• 機能のキーワード: haloacid dehalogenase, had, hydrolase
• 由来する生物種: SULFOLOBUS TOKODAII
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48145.36

構造登録者

Rye, C.A.,Isupov, M.N.,Lebedev, A.A.,Littlechild, J.A. (登録日: 2008-10-13, 公開日: 2008-12-09, 最終更新日: 2023-12-13)

主引用文献

Rye, C.A.,Isupov, M.N.,Lebedev, A.A.,Littlechild, J.A.
Biochemical and Structural Studies of a L-Haloacid Dehalogenase from the Thermophilic Archaeon Sulfolobus Tokodaii.
Extremophiles, 13:179-, 2009

PubMed Abstract: Haloacid dehalogenases have potential applications in the pharmaceutical and fine chemical industry as well as in the remediation of contaminated land. The L: -2-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii has been cloned and over-expressed in Escherichia coli and successfully purified to homogeneity. Here we report the structure of the recombinant dehalogenase solved by molecular replacement in two different crystal forms. The enzyme is a homodimer with each monomer being composed of a core-domain of a beta-sheet bundle surrounded by alpha-helices and an alpha-helical sub-domain. This fold is similar to previously solved mesophilic L: -haloacid dehalogenase structures. The monoclinic crystal form contains a putative inhibitor L: -lactate in the active site. The enzyme displays haloacid dehalogenase activity towards carboxylic acids with the halide attached at the C2 position with the highest activity towards chloropropionic acid. The enzyme is thermostable with maximum activity at 60 degrees C and a half-life of over 1 h at 70 degrees C. The enzyme is relatively stable to solvents with 25% activity lost when incubated for 1 h in 20% v/v DMSO.

PubMed: 19039518
DOI: 10.1007/S00792-008-0208-0

実験手法

X-RAY DIFFRACTION (1.9 Å)