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Crystal structure of the cold‐adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5
Author(s) -
Tratsiak Katsiaryna,
Prudnikova Tatyana,
Drienovska Ivana,
Damborsky Jiri,
Brynda Jiri,
Pachl Petr,
Kuty Michal,
Chaloupkova Radka,
Rezacova Pavlina,
Kuta Smatanova Ivana
Publication year - 2019
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x19002796
Subject(s) - dehalogenase , chemistry , enzyme , hydrolase , subfamily , biosensor , stereochemistry , crystallography , biochemistry , gene
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.