Crystallization and Preliminary X-ray Analysis of a Novel Haloalkane Dehalogenase DbeA from Bradyrhizobium elkani USDA94
Prudnikova, T., Mozga, T., Rezacova, P., Chaloupkova, R., Sato, Y., Nagata, Y., Brynda, J., Kuty, M., Damborsky, J., Kuta Smatanova, I.
ACTA CRYSTALLOGRAPHICA F65: 353-356 (2009)
A novel enzyme, DbeA, belonging to the haloalkane dehalogenase family (EC 188.8.131.52) 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 P212121, while the crystals of DbeA1 belonged to the monoclinic space group C2. Diffraction data were collected to 2.2 Å resolution for both DbeA and DbeA1 crystals.