7BFR

Thermogutta terrifontis esterase 2 phosphorylated by paraoxon

7BFR の概要

• エントリーDOI: 10.2210/pdb7bfr/pdb
• 関連するPDBエントリー: 7bfn
• 分子名称: Esterase, CARBONATE ION (3 entities in total)
• 機能のキーワード: nerve agent, conjugate, esterase, hydrolase
• 由来する生物種: Thermogutta terrifontis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31783.00

構造登録者

Brazzolotto, X.B.,Bzdrenga, J.,Nachon, F. (登録日: 2021-01-04, 公開日: 2021-02-10, 最終更新日: 2024-01-31)

主引用文献

Bzdrenga, J.,Trenet, E.,Chantegreil, F.,Bernal, K.,Nachon, F.,Brazzolotto, X.
A Thermophilic Bacterial Esterase for Scavenging Nerve Agents: A Kinetic, Biophysical and Structural Study.
Molecules, 26:-, 2021

PubMed Abstract: Organophosphorous nerve agents (OPNA) pose an actual and major threat for both military and civilians alike, as an upsurge in their use has been observed in the recent years. Currently available treatments mitigate the effect of the nerve agents, and could be vastly improved by means of scavengers of the nerve agents. Consequently, efforts have been made over the years into investigating enzymes, also known as bioscavengers, which have the potential either to trap or hydrolyze these toxic compounds. We investigated the previously described esterase 2 from (TtEst2) as a potential bioscavenger of nerve agents. As such, we assessed its potential against G-agents (tabun, sarin, and cyclosarin), VX, as well as the pesticide paraoxon. We report that TtEst2 is a good bioscavenger of paraoxon and G-agents, but is rather slow at scavenging VX. X-ray crystallography studies showed that TtEst2 forms an irreversible complex with the aforementioned agents, and allowed the identification of amino-acids, whose mutagenesis could lead to better scavenging properties for VX. In conjunction with its cheap production and purification processes, as well as a robust structural backbone, further engineering of TtEst2 could lead to a stopgap bioscavenger useful for in corpo scavenging or skin decontamination.

PubMed: 33513869
DOI: 10.3390/molecules26030657

実験手法

X-RAY DIFFRACTION (1.99 Å)