5VEJ

High resolution crystal structure of a fluoride-inhibited organo-phosphate-degrading metallohydrolase

5VEJ の概要

• エントリーDOI: 10.2210/pdb5vej/pdb
• 分子名称: Phosphotriesterase, ACETATE ION, COBALT (II) ION, ... (5 entities in total)
• 機能のキーワード: metallohydrolase, fluoride, inhibited, organo-phosphate-degrading, hydrolase
• 由来する生物種: Rhizobium radiobacter (Agrobacterium tumefaciens)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35843.48

構造登録者

Selleck, C. (登録日: 2017-04-04, 公開日: 2017-07-19, 最終更新日: 2023-11-15)

主引用文献

Selleck, C.,Guddat, L.W.,Ollis, D.L.,Schenk, G.,Pedroso, M.M.
High resolution crystal structure of a fluoride-inhibited organophosphate-degrading metallohydrolase.
J. Inorg. Biochem., 177:287-290, 2017

PubMed Abstract: Metal ion-dependent, organophosphate-degrading enzymes (OP hydrolases) have received increasing attention due to their ability to degrade and thus detoxify commonly used pesticides and nerve agents such as sarin and VX. These enzymes thus garner strong potential as bioremediators. The OP hydrolase from Agrobacterium radiobacter (OpdA) is one of the most efficient members of this group of enzymes. Previous studies have indicated that the choice of the hydrolysis-initiating nucleophile may depend on the pH of the reaction, with a metal ion-bridging hydroxide being preferred at lower pH (i.e. pH≤8.5), and a terminally coordinated hydroxide at higher pH (i.e. pH>9.0). Furthermore, fluoride was shown to be a potent inhibitor of the reaction, but only at low pH. Here, the crystal structure (1.3Å, pH6) of OpdA in presence of fluoride is described. While the first coordination sphere in the active site displays minimal changes in the presence of fluoride, the hydrogen bonding network that connects the dimetallic metal center to the substrate binding pocket is disrupted. Thus, the structure of fluoride-inhibited OpdA demonstrates the significance of this hydrogen bond network in controlling the mechanism and function of this enzyme.

PubMed: 28673485
DOI: 10.1016/j.jinorgbio.2017.06.013

実験手法

X-RAY DIFFRACTION (1.301 Å)