Open AccessCrystallization and preliminary X‐ray analysis of a novel haloalkane dehalogenase DbeA from Bradyrhizobium elkani USDA94
Author(s) -
Prudnikova Tatyana,
Mozga Tomas,
Rezacova Pavlina,
Chaloupkova Radka,
Sato Yukari,
Nagata Yuji,
Brynda Jiri,
Kuty Michal,
Damborsky Jiri,
Kuta Smatanova Ivana
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109007039
Subject(s) - orthorhombic crystal system , crystallography , chemistry , enzyme , stereochemistry , monoclinic crystal system , biology , biochemistry , crystal structure
A novel enzyme, DbeA, belonging to the haloalkane dehalogenase family (EC 3.8.1.5) was isolated from Bradyrhizobium elkani USDA94. This haloalkane dehalogenase is closely related to the DbjA enzyme from B. japonicum USDA110 (71% sequence identity), but has different biochemical properties. DbeA is generally less active and has a higher specificity towards brominated and iodinated compounds than DbjA. In order to understand the altered activity and specificity of DbeA, its mutant variant DbeA1, which carries the unique fragment of DbjA, was also constructed. Both wild‐type DbeA and DbeA1 were crystallized using the sitting‐drop vapour‐diffusion method. The crystals of DbeA belonged to the primitive orthorhombic space group P 2 1 2 1 2 1 , while the crystals of DbeA1 belonged to the monoclinic space group C 2. Diffraction data were collected to 2.2 Å resolution for both DbeA and DbeA1 crystals.