The tetrameric structure of the novel haloalkane dehalogenase DpaA from Paraglaciecola agarilytica NO2

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 molecu...

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Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2021-03, Vol.77 (3), p.347-356
Main Authors: Mazur, Andrii, Prudnikova, Tatyana, Grinkevich, Pavel, Mesters, Jeroen R., Mrazova, Daria, Chaloupkova, Radka, Damborsky, Jiri, Kuty, Michal, Kolenko, Petr, Kuta Smatanova, Ivana
Format: Article
Language:English
Subjects:
Bioremediation
Biosensors
Catalysis
Crystallization
Crystals
Data analysis
Diffraction
DpaA
Enzymes
Haloalkane dehalogenase
haloalkane dehalogenases
halogenated pollutants
Microorganisms
Nitrogen dioxide
oligomerization
Pollutants
tetrameric structure
Twinning
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Summary: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 Å 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. DpaA from P. agarilytica NO2, a novel type of haloalkane dehalogenase, was successfully purified and crystallized. The model of DpaA based on the crystallographic data reported here provides the first example of a tetrameric structure in haloalkane dehalogenase subfamily I.
ISSN:2059-7983
0907-4449
2059-7983
1399-0047
DOI:10.1107/S2059798321000486