6F9O

Crystal structure of cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5

6F9O の概要

• エントリーDOI: 10.2210/pdb6f9o/pdb
• 分子名称: Haloalkane dehalogenase, CHLORIDE ION, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• 機能のキーワード: microbial enzymes, haloalkane dehalogenases, hlds, alpha/beta-hydrolase fold enzymes, hydrolase, 2 domains, the highest activity towards 1-bromobutane, 1-bromohexane and 1, 3-dibromopropane
• 由来する生物種: Psychrobacter cryohalolentis (strain K5)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35537.60

構造登録者

Tratsiak, K.,Prudnikova, T.,Drienovska, I.,Damborsky, J.,Brynda, J.,Pachl, P.,Kuty, M.,Chaloupkova, R.,Kuta Smatanova, I.,Rezacova, P. (登録日: 2017-12-15, 公開日: 2019-02-27, 最終更新日: 2024-01-17)

主引用文献

Tratsiak, K.,Prudnikova, T.,Drienovska, I.,Damborsky, J.,Brynda, J.,Pachl, P.,Kuty, M.,Chaloupkova, R.,Rezacova, P.,Kuta Smatanova, I.
Crystal structure of the cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5.
Acta Crystallogr.,Sect.F, 75:324-331, 2019

PubMed Abstract: 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 Å. 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°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 α4 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.

PubMed: 31045561
DOI: 10.1107/S2053230X19002796

実験手法

X-RAY DIFFRACTION (1.05 Å)