Crystallization and Preliminary X-ray Diffraction Analysis of the Wild-Type Haloalkane Dehalogenase DhaA and its Variant DhaA13 Complexed with Different Ligands
| Authors | |
|---|---|
| Year of publication | 2011 |
| Type | Article in Periodical |
| Magazine / Source | Acta Crystallographica F |
| MU Faculty or unit | |
| Citation | |
| Doi | http://dx.doi.org/10.1107/S1744309110051286 |
| Field | Biochemistry |
| Keywords | Crystallization; X-ray Diffraction Analysis; Haloalkane Dehalogenase DhaA |
| Description | Haloalkane dehalogenases make up an important class of hydrolytic enzymes which catalyse the cleavage of carbon-halogen bonds in halogenated aliphatic compounds. There is growing interest in these enzymes owing to their potential use in environmental and industrial applications. The haloalkane dehalogenase DhaA fromRhodococcus rhodochrous NCIMB 13064 can slowly detoxify the industrial pollutant 1,2,3-trichloropropane (TCP). Structural analysis of this enzyme complexed with target ligands was conducted in order to obtain detailed information about the structural limitations of its catalytic properties. In this study, the crystallization and preliminary X-ray analysis of complexes of wild-type DhaA with 2-propanol and with TCP and of complexes of the catalytically inactive variant DhaA13 with the dye coumarin and with TCP are described. |
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