Atomic resolution studies of haloalkane dehalogenases DhaA04, DhaA14 and DhaA15 with engineered access tunnels.

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Authors	STSIAPANAVA Alena DOHNÁLEK J. GAVIRA J. KUTÝ Michal KOUDELÁKOVÁ Táňa DAMBORSKÝ Jiří KUTÁ-SMATANOVÁ Ivana
Year of publication	2010
Type	Article in Periodical
Magazine / Source	ACTA CRYSTALLOGRAPHICA D
MU Faculty or unit	Faculty of Science
Citation
Web	http://loschmidt.chemi.muni.cz/peg/pdf/acsf10a.pdf
Field	Biochemistry
Keywords	haloalkane dehalogenase DhaA ; Rhodococcus rhodochrous NCIMB 13064; hydrolytic degradation; 1.2.3-trichloropropane (TCP)
Description	The haloalkane dehalogenase DhaA from Rhodococcus rhodochrous NCIMB 13064 is a bacterial enzyme that shows catalytic activity for the hydrolytic degradation of the highly toxic industrial pollutant 1,2,3-trichloropropane (TCP). Mutagenesis focused on the access tunnels of DhaA produced protein variants with significantly improved activity towards TCP. Three mutants of DhaA named DhaA04 (C176Y), DhaA14 (I135F) and DhaA15 (C176Y + I135F) were constructed in order to study the functional relevance of the tunnels connecting the buried active site of the protein with the surrounding solvent. All three protein variants were crystallized using the sitting-drop vapour-diffusion technique.
Related projects:	Proteins in metabolism and interaction of organisms with the environment Interactions among the chemicals, environment and biological systems and their consequences on the global, regional and local scales (INCHEMBIOL) Center of Biocatalysis and Biotransformation