6F9O
Crystal structure of cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5
Summary for 6F9O
| Entry DOI | 10.2210/pdb6f9o/pdb |
| Descriptor | Haloalkane dehalogenase, CHLORIDE ION, DI(HYDROXYETHYL)ETHER, ... (5 entities in total) |
| Functional Keywords | microbial enzymes, haloalkane dehalogenases, hlds, alpha/beta-hydrolase fold enzymes, hydrolase, 2 domains, the highest activity towards 1-bromobutane, 1-bromohexane and 1, 3-dibromopropane |
| Biological source | Psychrobacter cryohalolentis (strain K5) |
| Total number of polymer chains | 1 |
| Total formula weight | 35537.60 |
| Authors | Tratsiak, K.,Prudnikova, T.,Drienovska, I.,Damborsky, J.,Brynda, J.,Pachl, P.,Kuty, M.,Chaloupkova, R.,Kuta Smatanova, I.,Rezacova, P. (deposition date: 2017-12-15, release date: 2019-02-27, Last modification date: 2024-01-17) |
| Primary citation | Tratsiak, K.,Prudnikova, T.,Drienovska, I.,Damborsky, J.,Brynda, J.,Pachl, P.,Kuty, M.,Chaloupkova, R.,Rezacova, P.,Kuta Smatanova, I. Crystal structure of the cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5. Acta Crystallogr.,Sect.F, 75:324-331, 2019 Cited by PubMed Abstract: 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 Å. 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°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 α4 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. PubMed: 31045561DOI: 10.1107/S2053230X19002796 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.05 Å) |
Structure validation
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