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Crystal structure of the cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5
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SYSNO ASEP 0505903 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Crystal structure of the cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5 Author(s) Tratsiak, K. (CZ)
Prudnikova, Tatyana (MBU-M)
Drienovská, I. (CZ)
Damborský, J. (CZ)
Brynda, Jiří (UMG-J) RID
Pachl, P. (CZ)
Kutý, Michal (MBU-M) ORCID
Chaloupková, R. (CZ)
Řezáčová, Pavlína (UMG-J) RID
Kutá Smatanová, Ivana (MBU-M) ORCIDNumber of authors 10 Source Title Acta Crystallographica Section F-Structural Biology Communications
Roč. 75, Pt 5 (2019), s. 324-331Number of pages 8 s. Publication form Print - P Language eng - English Country US - United States Keywords haloalkane dehalogenase ; alpha/beta-hydrolase ; X-ray diffraction ; psychrophiles ; structural analysis ; Psychrobacter cryohalolentis Subject RIV EB - Genetics ; Molecular Biology OECD category Biophysics Subject RIV - cooperation Institute of Microbiology - Biochemistry Method of publishing Limited access Institutional support UMG-J - RVO:68378050 ; MBU-M - RVO:61388971 UT WOS 000466795900002 DOI 10.1107/S2053230X19002796 Annotation 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. Workplace Institute of Molecular Genetics Contact Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Year of Publishing 2020 Electronic address http://scripts.iucr.org/cgi-bin/paper?S2053230X19002796
Number of the records: 1