Knowledge of the structure of proteins is a key in identifying and describing the detailed mechanism of biological processes, the development of therapeutics, the degradation of pollutants from the environment, etc. One of the methods used to determine the structure of proteins on atomic resolution is X-ray crystallography. For many years, our laboratory has been researching structures of different types and mutant variants of haloalkane dehalogenases (HLDs). HLDs are microbial enzymes exhibiting catalytic activity for the hydrolytic conversion of xenobiotics and toxic halogenated aliphatic compounds to the corresponding alcohols. To date, several tertiary structures of these enzymes have been solving by X-ray diffraction analysis. Although we have several types of newly cloned enzymes and their mutants, crystallize and structurally characterize these enzymes is not trivial. In the lecture will be discussed the complications in the preparation of crystals, the enzyme structures will be described and the reaction mechanism of the dehalogenation reaction will be outlined.
This research is supporting by the GACR (17-24321S).