4Q3K

Crystal structure of MGS-M1, an alpha/beta hydrolase enzyme from a Medee basin deep-sea metagenome library

4Q3K の概要

• エントリーDOI: 10.2210/pdb4q3k/pdb
• 関連するPDBエントリー: 4Q3L 4Q3M 4Q3N 4Q3O
• 分子名称: MGS-M1, CHLORIDE ION, FLUORIDE ION, ... (5 entities in total)
• 機能のキーワード: metagenome, metagenomic library, alpha and beta proteins, alpha/beta hydrolase superfamily, esterase/lipase fold, hydrolase
• 由来する生物種: unidentified
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59088.13

構造登録者

Stogios, P.J.,Xu, X.,Cui, H.,Alcaide, M.,Ferrer, M.,Savchenko, A. (登録日: 2014-04-11, 公開日: 2015-02-25, 最終更新日: 2023-09-20)

主引用文献

Alcaide, M.,Stogios, P.J.,Lafraya, A.,Tchigvintsev, A.,Flick, R.,Bargiela, R.,Chernikova, T.N.,Reva, O.N.,Hai, T.,Leggewie, C.C.,Katzke, N.,La Cono, V.,Matesanz, R.,Jebbar, M.,Jaeger, K.E.,Yakimov, M.M.,Yakunin, A.F.,Golyshin, P.N.,Golyshina, O.V.,Savchenko, A.,Ferrer, M.
Pressure adaptation is linked to thermal adaptation in salt-saturated marine habitats.
Environ Microbiol, 17:332-345, 2015

PubMed Abstract: The present study provides a deeper view of protein functionality as a function of temperature, salt and pressure in deep-sea habitats. A set of eight different enzymes from five distinct deep-sea (3040-4908 m depth), moderately warm (14.0-16.5°C) biotopes, characterized by a wide range of salinities (39-348 practical salinity units), were investigated for this purpose. An enzyme from a 'superficial' marine hydrothermal habitat (65°C) was isolated and characterized for comparative purposes. We report here the first experimental evidence suggesting that in salt-saturated deep-sea habitats, the adaptation to high pressure is linked to high thermal resistance (P value = 0.0036). Salinity might therefore increase the temperature window for enzyme activity, and possibly microbial growth, in deep-sea habitats. As an example, Lake Medee, the largest hypersaline deep-sea anoxic lake of the Eastern Mediterranean Sea, where the water temperature is never higher than 16°C, was shown to contain halopiezophilic-like enzymes that are most active at 70°C and with denaturing temperatures of 71.4°C. The determination of the crystal structures of five proteins revealed unknown molecular mechanisms involved in protein adaptation to poly-extremes as well as distinct active site architectures and substrate preferences relative to other structurally characterized enzymes.

PubMed: 25330254
DOI: 10.1111/1462-2920.12660

実験手法

X-RAY DIFFRACTION (1.57 Å)