7AVR

The tetrameric structure of haloalkane dehalogenase DpaA from Paraglaciecola agarilytica NO2

7AVR の概要

• エントリーDOI: 10.2210/pdb7avr/pdb
• 分子名称: Haloalkane dehalogenase 1, CHLORIDE ION (3 entities in total)
• 機能のキーワード: haloalkane dehalogenase, enzyme, tetramer, hydrolase
• 由来する生物種: Paraglaciecola agarilytica NO2
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 276856.78

構造登録者

Mazur, A.,Kolenko, P.,Prudnikova, T.,Grinkevich, P.,Kuta Smatanova, I. (登録日: 2020-11-05, 公開日: 2021-03-17, 最終更新日: 2024-01-31)

主引用文献

Mazur, A.,Prudnikova, T.,Grinkevich, P.,Mesters, J.R.,Mrazova, D.,Chaloupkova, R.,Damborsky, J.,Kuty, M.,Kolenko, P.,Kuta Smatanova, I.
The tetrameric structure of the novel haloalkane dehalogenase DpaA from Paraglaciecola agarilytica NO2.
Acta Crystallogr D Struct Biol, 77:347-356, 2021

PubMed Abstract: 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.

PubMed: 33645538
DOI: 10.1107/S2059798321000486

実験手法

X-RAY DIFFRACTION (2 Å)