Crystallization and Crystallographic Analysis of the Rhodococcus rhodochrous NCIMB 13064 Mutant DhaA31 and its Complex with 1,2,3-Trichloropropane
Authors
Lahoda, M., Chaloupková, R., Stsiapanava, A., Damborský, J., Kutá Smatanová, I.
Source
Acta Crystallographica 67
Abstract
Haloalkane dehalogenases hydrolyze carbon-halogen bonds in a wide range of halogenated aliphatic compounds. The potential use of haloalkane dehalogenases in bioremediation applications has stimulated intensive investigation of these enzymes and their engineering. The mutant DhaA31 was constructed to degrade the anthropogenic compound 1,2,3-trichloropropane (TCP) using a new strategy. This strategy enhances activity towards TCP by decreasing the accessibility of the active site to water molecules, thereby promoting formation of the activated complex. The structure of DhaA31 will help in understanding the structure-function relationships involved in the improved dehalogenation of TCP. The mutant protein DhaA31 was crystallized by the sitting-drop vapour-diffusion technique and crystals of DhaA31 in complex with TCP were obtained using soaking experiments. Both crystals belonged to the triclinic space group P1. Diffraction data were collected to high resolution: to 1.31 Å for DhaA31 and to 1.26 Å for DhaA31 complexed with TCP.
Source
Lahoda, M., Chaloupková, R., Stsiapanava, A., Damborský, J., Kutá Smatanová, I.:
Crystallization and Crystallographic Analysis of the Rhodococcus rhodochrous NCIMB 13064 Mutant DhaA31 and its Complex with 1,2,3-Trichloropropane,
Acta Crystallographica , 67, 397-400, 2011.
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