Structural studies of haloacid dehalogenase Tt81 from Thermococcus thioreducens

Kristyna Rejzkova¹, Tatyana Prudnikova^1,2, Michal Kuty^1,2, Radka Chaloupkova³, Jiri Damborsky³, Ivana Kuta Smatanova^1,2

¹University of South Bohemia in Ceske Budejovice, Faculty of Science, Branisovska 1760, 370 05 Ceske Budejovice
²Academy of Science of the Czech Republic, Center for Nanobiology and Structural Biology IMB, Zamek 136, 373 33 Nove Hrady
³1Loschmidt Laboratories, Department of Experimental Biology and Research Centre for Toxic Compounds in the Environment RECETOX, Faculty of Science, Masaryk University, Kamenice 5/A13, 625 00 Brno, Czech Republic

Industrial production and the chemical industry are responsible for the growing number of foreign substances (xenobiotics) in the biosphere. Although the metabolic versatility of microbial communities is enormous, it is not always that xenobiotics degrade. Substitution of halogens can lead to an increase in the toxicity of halogenated organic compounds, which represent a significant proportion of industrially used solvents, herbicides and pesticides. These substances have become the target of a number of bioremediation research projects aimed at removing xenobiotics from infested areas, for example by the action of living organisms. Dehalogenases, microbial enzymes capable of cleaving a carbon-halogen bond, have been shown to be useful. Dehalogenases include several groups of enzymes such as haloacid dehalogenases. Haloacid dehalogenase Tt81 was isolated from an extremely thermophilic and anaerobic bacteria Thermococcus thioreducens,  that lives in hydrothermal springs, areas deep underground and oil wells. The purified protein Tt81 was used for crystallization experiments. Sitting drop vapour diffusion and microbatch under oil where used as crystallization methods. The obtained crystals were subjected to X-ray diffraction and diffraction data will be used for further research focused on structure determination.

The work was supported from GACR 17-24321S.