Crystallization and preliminary X-ray analysis of a novel haloalkane dehalogenase DbeA from bradyrhizobium elkani USDA94

Tatyana Prudnikova, Tomas Mozga, Pavlina Rezacova, Radka Chaloupkova, Yukari Sato, Yuji Nagata, Jiri Brynda, Michal Kuty, Jiri Damborsky, Ivana Kuta Smatanova

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)

Abstract

A novel enzyme, DbeA, belonging to the haloalkane dehalogenase family (EC 3.8.1.5) was isolated from Bradyrhizobium elkani USDA94. This halo-alkane 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.

Original languageEnglish
Pages (from-to)353-356
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume65
Issue number4
DOIs
Publication statusPublished - 2009

Keywords

  • Bradyrhizobium elkani USDA94
  • DbeA
  • Haloalkane dehalogenases

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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