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@article{1790208,
author = {Mazur, Andrii and Prudnikova, Tanyana and Grinkevich, Pavel and Mesters, Jeroen R. and Mrazova, Daria and Chaloupková, Radka and Damborský, Jiří and Kuty, Michal and Kolenko, Petr and Kuta Smatanova, Ivana},
article_location = {Chester},
article_number = {March 2021},
doi = {http://dx.doi.org/10.1107/S2059798321000486},
keywords = {DpaA; crystallization; haloalkane dehalogenases; halogenated pollutants; tetrameric structure; oligomerization},
language = {eng},
issn = {2059-7983},
journal = {Acta Crystallographica Section D: Structural Biology},
title = {The tetrameric structure of the novel haloalkane dehalogenase DpaA from Paraglaciecola agarilytica NO2},
url = {https://scripts.iucr.org/cgi-bin/paper?S2059798321000486},
volume = {77},
year = {2021}
}
TY - JOUR
ID - 1790208
AU - Mazur, Andrii - Prudnikova, Tanyana - Grinkevich, Pavel - Mesters, Jeroen R. - Mrazova, Daria - Chaloupková, Radka - Damborský, Jiří - Kuty, Michal - Kolenko, Petr - Kuta Smatanova, Ivana
PY - 2021
TI - The tetrameric structure of the novel haloalkane dehalogenase DpaA from Paraglaciecola agarilytica NO2
JF - Acta Crystallographica Section D: Structural Biology
VL - 77
IS - March 2021
SP - 347-356
EP - 347-356
PB - International Union of Crystallography
SN - 20597983
KW - DpaA
KW - crystallization
KW - haloalkane dehalogenases
KW - halogenated pollutants
KW - tetrameric structure
KW - oligomerization
UR - https://scripts.iucr.org/cgi-bin/paper?S2059798321000486
N2 - Haloalkane dehalogenases (EC 3.8.1.5) are microbial enzymes that catalyse the hydrolytic conversion of halogenated compounds, resulting in a halide ion, a proton and an alcohol. These enzymes are used in industrial biocatalysis, bioremediation and biosensing of environmental pollutants or for molecular tagging in cell biology. The novel haloalkane dehalogenase DpaA described here was isolated from the psychrophilic and halophilic bacterium Paraglaciecola agarilytica NO2, which was found in marine sediment collected from the East Sea near Korea. Gel-filtration experiments and size-exclusion chromatography provided information about the dimeric composition of the enzyme in solution. The DpaA enzyme was crystallized using the sitting-drop vapour-diffusion method, yielding rod-like crystals that diffracted X-rays to 2.0 angstrom resolution. Diffraction data analysis revealed a case of merohedral twinning, and subsequent structure modelling and refinement resulted in a tetrameric model of DpaA, highlighting an uncommon multimeric nature for a protein belonging to haloalkane dehalogenase subfamily I.
ER -
MAZUR, Andrii, Tanyana PRUDNIKOVA, Pavel GRINKEVICH, Jeroen R. MESTERS, Daria MRAZOVA, Radka CHALOUPKOVÁ, Jiří DAMBORSKÝ, Michal KUTY, Petr KOLENKO and Ivana KUTA SMATANOVA. The tetrameric structure of the novel haloalkane dehalogenase DpaA from Paraglaciecola agarilytica NO2. \textit{Acta Crystallographica Section D: Structural Biology}. Chester: International Union of Crystallography, 2021, vol.~77, March 2021, p.~347-356. ISSN~2059-7983. Available from: https://dx.doi.org/10.1107/S2059798321000486.
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