7B4Q

Structure of a cold active HSL family esterase reveals mechanisms of low temperature adaptation and substrate specificity

7B4Q の概要

• エントリーDOI: 10.2210/pdb7b4q/pdb
• 分子名称: Lipase, 1,2-ETHANEDIOL, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: bacillus cohnii, esterase, low temperature adapted, regio-selective esterase, hormone-sensitive family, hydrolase, lipase
• 由来する生物種: Bacillus cohnii NBRC 15565
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 71535.45

構造登録者

Rizkallah, P.J.,Jones, D.D.,Noby, N.,Auhim, H. (登録日: 2020-12-02, 公開日: 2021-12-15, 最終更新日: 2024-01-31)

主引用文献

Noby, N.,Auhim, H.S.,Winter, S.,Worthy, H.L.,Embaby, A.M.,Saeed, H.,Hussein, A.,Pudney, C.R.,Rizkallah, P.J.,Wells, S.A.,Jones, D.D.
Structure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism.
Open Biology, 11:210182-210182, 2021

PubMed Abstract: Here we determined the structure of a cold active family IV esterase (EstN7) cloned strain N1. EstN7 is a dimer with a classical α/β hydrolase fold. It has an acidic surface that is thought to play a role in cold-adaption by retaining solvation under changed water solvent entropy at lower temperatures. The conformation of the functionally important cap region is significantly different to EstN7's closest relatives, forming a bridge-like structure with reduced helical content providing greater access to the active site through more than one substrate access tunnel. However, dynamics do not appear to play a major role in cold adaption. Molecular dynamics at different temperatures, rigidity analysis, normal mode analysis and geometric simulations of motion confirm the flexibility of the cap region but suggest that the rest of the protein is largely rigid. Rigidity analysis indicates the distribution of hydrophobic tethers is appropriate to colder conditions, where the hydrophobic effect is weaker than in mesophilic conditions due to reduced water entropy. Thus, it is likely that increased substrate accessibility and tolerance to changes in water entropy are important for of EstN7's cold adaptation rather than changes in dynamics.

PubMed: 34847772
DOI: 10.1098/rsob.210182

実験手法

X-RAY DIFFRACTION (1.61 Å)