3BJX

Structure of a Group I haloacid dehalogenase from Pseudomonas putida strain PP3

3BJX の概要

• エントリーDOI: 10.2210/pdb3bjx/pdb
• 分子名称: Halocarboxylic acid dehalogenase DehI, SULFATE ION (3 entities in total)
• 機能のキーワード: plasmid, hydrolase
• 由来する生物種: Pseudomonas putida
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 141003.54

構造登録者

Schmidberger, J.W.,Wilce, M.C.J. (登録日: 2007-12-05, 公開日: 2008-04-01, 最終更新日: 2024-10-30)

主引用文献

Schmidberger, J.W.,Wilce, J.A.,Weightman, A.J.,Whisstock, J.C.,Wilce, M.C.J.
The crystal structure of DehI reveals a new alpha-haloacid dehalogenase fold and active-site mechanism
J.Mol.Biol., 378:284-294, 2008

PubMed Abstract: Haloacid dehalogenases catalyse the removal of halides from organic haloacids and are of interest for bioremediation and for their potential use in the synthesis of industrial chemicals. We present the crystal structure of the homodimer DehI from Pseudomonas putida strain PP3, the first structure of a group I alpha-haloacid dehalogenase that can process both L- and D-substrates. The structure shows that the DehI monomer consists of two domains of approximately 130 amino acids that have approximately 16% sequence identity yet adopt virtually identical and unique folds that form a pseudo-dimer. Analysis of the active site reveals the likely binding mode of both L- and D-substrates with respect to key catalytic residues. Asp189 is predicted to activate a water molecule for nucleophilic attack of the substrate chiral centre resulting in an inversion of configuration of either l- or d-substrates in contrast to D-only enzymes. These details will assist with future bioengineering of dehalogenases.

PubMed: 18353360
DOI: 10.1016/j.jmb.2008.02.035

実験手法

X-RAY DIFFRACTION (2.3 Å)