Crystal structure of the cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5
| Autoři | |
|---|---|
| Rok publikování | 2019 |
| Druh | Článek v odborném periodiku |
| Časopis / Zdroj | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS |
| Fakulta / Pracoviště MU | |
| Citace | |
| www | http://scripts.iucr.org/cgi-bin/paper?S2053230X19002796 |
| Doi | http://dx.doi.org/10.1107/S2053230X19002796 |
| Klíčová slova | haloalkane dehalogenase; alpha/beta-hydrolase; X-ray diffraction; psychrophiles; structural analysis; Psychrobacter cryohalolentis |
| Popis | Haloalkane dehalogenases (HLDs) convert halogenated aliphatic pollutants to less toxic compounds by a hydrolytic mechanism. Owing to their broad substrate specificity and high enantioselectivity, haloalkane dehalogenases can function as biosensors to detect toxic compounds in the environment or can be used for the production of optically pure compounds. Here, the structural analysis of the haloalkane dehalogenase DpcA isolated from the psychrophilic bacterium Psychrobacter cryohalolentis K5 is presented at the atomic resolution of 1.05 angstrom. This enzyme exhibits a low temperature optimum, making it attractive for environmental applications such as biosensing at the subsurface environment, where the temperature typically does not exceed 25 degrees C. The structure revealed that DpcA possesses the shortest access tunnel and one of the most widely open main tunnels among structural homologs of the HLD-I subfamily. Comparative analysis revealed major differences in the region of the alpha 4 helix of the cap domain, which is one of the key determinants of the anatomy of the tunnels. The crystal structure of DpcA will contribute to better understanding of the structure-function relationships of cold-adapted enzymes. |
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