| TRATSIAK, K., Tanyana PRUDNIKOVA, Ivana DRIENOVSKÁ, Jiří DAMBORSKÝ, Jiří BRYNDA, Petr PACHL, Michal KUTÝ, Radka CHALOUPKOVÁ, P. REZACOVA and I.K. SMATANOVA. Crystal structure of the cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS. CHESTER: INT UNION CRYSTALLOGRAPHY, 2019, vol. 75, MAY 2019, p. 324-331. ISSN 2053-230X. Available from: https://dx.doi.org/10.1107/S2053230X19002796. |
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@article{1638976,
author = {Tratsiak, K. and Prudnikova, Tanyana and Drienovská, Ivana and Damborský, Jiří and Brynda, Jiří and Pachl, Petr and Kutý, Michal and Chaloupková, Radka and Rezacova, P. and Smatanova, I.K.},
article_location = {CHESTER},
article_number = {MAY 2019},
doi = {http://dx.doi.org/10.1107/S2053230X19002796},
keywords = {haloalkane dehalogenase; alpha/beta-hydrolase; X-ray diffraction; psychrophiles; structural analysis; Psychrobacter cryohalolentis},
language = {eng},
issn = {2053-230X},
journal = {ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS},
title = {Crystal structure of the cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5},
url = {http://scripts.iucr.org/cgi-bin/paper?S2053230X19002796},
volume = {75},
year = {2019}
}
TY - JOUR
ID - 1638976
AU - Tratsiak, K. - Prudnikova, Tanyana - Drienovská, Ivana - Damborský, Jiří - Brynda, Jiří - Pachl, Petr - Kutý, Michal - Chaloupková, Radka - Rezacova, P. - Smatanova, I.K.
PY - 2019
TI - Crystal structure of the cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5
JF - ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
VL - 75
IS - MAY 2019
SP - 324-331
EP - 324-331
PB - INT UNION CRYSTALLOGRAPHY
SN - 2053230X
KW - haloalkane dehalogenase
KW - alpha/beta-hydrolase
KW - X-ray diffraction
KW - psychrophiles
KW - structural analysis
KW - Psychrobacter cryohalolentis
UR - http://scripts.iucr.org/cgi-bin/paper?S2053230X19002796
L2 - http://scripts.iucr.org/cgi-bin/paper?S2053230X19002796
N2 - 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.
ER -
TRATSIAK, K., Tanyana PRUDNIKOVA, Ivana DRIENOVSKÁ, Jiří DAMBORSKÝ, Jiří BRYNDA, Petr PACHL, Michal KUTÝ, Radka CHALOUPKOVÁ, P. REZACOVA and I.K. SMATANOVA. Crystal structure of the cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5. \textit{ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS}. CHESTER: INT UNION CRYSTALLOGRAPHY, 2019, vol.~75, MAY 2019, p.~324-331. ISSN~2053-230X. Available from: https://dx.doi.org/10.1107/S2053230X19002796.
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