1JUD

L-2-HALOACID DEHALOGENASE

1JUD の概要

• エントリーDOI: 10.2210/pdb1jud/pdb
• 分子名称: L-2-HALOACID DEHALOGENASE (2 entities in total)
• 機能のキーワード: dehalogenase, hydrolase
• 由来する生物種: Pseudomonas sp.
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26207.59

構造登録者

Hisano, T.,Hata, Y.,Fujii, T.,Liu, J.-Q.,Kurihara, T.,Esaki, N.,Soda, K. (登録日: 1996-06-03, 公開日: 1996-12-07, 最終更新日: 2024-02-07)

主引用文献

Hisano, T.,Hata, Y.,Fujii, T.,Liu, J.Q.,Kurihara, T.,Esaki, N.,Soda, K.
Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold.
J.Biol.Chem., 271:20322-20330, 1996

PubMed Abstract: L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. The crystal structure of the homodimeric enzyme from Pseudomonas sp. YL has been determined by a multiple isomorphous replacement method and refined at 2.5 A resolution to a crystallographic R-factor of 19.5%. The subunit consists of two structurally distinct domains: the core domain and the subdomain. The core domain has an alpha/beta structure formed by a six-stranded parallel beta-sheet flanked by five alpha-helices. The subdomain inserted into the core domain has a four helix bundle structure providing the greater part of the interface for dimer formation. There is an active site cavity between the domains. An experimentally identified nucleophilic residue, Asp-10, is located on a loop following the amino-terminal beta-strand in the core domain, and other functional residues, Thr-14, Arg-41, Ser-118, Lys-151, Tyr-157, Ser-175, Asn-177, and Asp-180, detected by a site-directed mutagenesis experiment, are arranged around the nucleophile in the active site. Although the enzyme is an alpha/beta-type hydrolase, it does not belong to the alpha/beta hydrolase fold family, from the viewpoint of the topological feature and the position of the nucleophile.

PubMed: 8702766
DOI: 10.1074/jbc.271.34.20322

実験手法

X-RAY DIFFRACTION (2.5 Å)