Hisano_1996_J.Biol.Chem_271_20322

Reference

Title : 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 - Hisano_1996_J.Biol.Chem_271_20322
Author(s) : Hisano T , Hata Y , Fujii T , Liu JQ , Kurihara T , Esaki N , Soda K
Ref : Journal of Biological Chemistry , 271 :20322 , 1996
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.
ESTHER : Hisano_1996_J.Biol.Chem_271_20322
PubMedSearch : Hisano_1996_J.Biol.Chem_271_20322
PubMedID: 8702766

Related information

Citations formats

Hisano T, Hata Y, Fujii T, Liu JQ, Kurihara T, Esaki N, Soda K (1996)
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
Journal of Biological Chemistry 271 :20322

Hisano T, Hata Y, Fujii T, Liu JQ, Kurihara T, Esaki N, Soda K (1996)
Journal of Biological Chemistry 271 :20322