Franken_1991_Embo.J_10_1297

Reference

Title : Crystal structure of haloalkane dehalogenase: an enzyme to detoxify halogenated alkanes - Franken_1991_EMBO.J_10_1297
Author(s) : Franken SM , Rozeboom HJ , Kalk KH , Dijkstra BW
Ref : EMBO Journal , 10 :1297 , 1991
Abstract :

Haloalkane dehalogenase from Xanthobacter autotrophicus GJ10 converts 1-haloalkanes to the corresponding alcohols and halide ions with water as the sole cosubstrate and without any need for oxygen or cofactors. The three-dimensional structure has been determined by multiple isomorphous replacement techniques using three heavy atom derivatives. The structure has been refined at 2.4 A resolution to an R-factor of 17.9%. The monomeric enzyme is a spherical molecule and is composed to two domains: domain I has an alpha/beta type structure with a central eight-stranded mainly parallel beta-sheet. Domain II lies like a cap on top of domain I and consists of alpha-helices connected by loops. Except for the cap domain the structure resembles that of the dienelactone hydrolase in spite of any significant sequence homology. The putative active site is completely buried in an internal hydrophobic cavity which is located between the two domains. From the analysis of the structure it is suggested that Asp124 is the nucleophilic residue essential for the catalysis. It interacts with His289 which is hydrogen-bonded to Asp260.

PubMedSearch : Franken_1991_EMBO.J_10_1297
PubMedID: 2026135
Gene_locus related to this paper: xanau-halo1

Related information

Gene_locus xanau-halo1
Family Haloalkane_dehalogenase-HLD1
Structure 2HAD

Citations formats

Franken SM, Rozeboom HJ, Kalk KH, Dijkstra BW (1991)
Crystal structure of haloalkane dehalogenase: an enzyme to detoxify halogenated alkanes
EMBO Journal 10 :1297

Franken SM, Rozeboom HJ, Kalk KH, Dijkstra BW (1991)
EMBO Journal 10 :1297