8UQY

Round 18 Arylesterase Variant of Phosphotriesterase Bound to Europium(III) Measured at 9.5 keV

8UQY の概要

• エントリーDOI: 10.2210/pdb8uqy/pdb
• 分子名称: Phosphotriesterase variant PTE-R18, (4S)-2-METHYL-2,4-PENTANEDIOL, EUROPIUM (III) ION, ... (5 entities in total)
• 機能のキーワード: phosphotriesterase, 9.5 kev, europium, hydrolase
• 由来する生物種: Brevundimonas diminuta
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73112.39

構造登録者

Breeze, C.W.,Frkic, R.L.,Campbell, E.C.,Jackson, C.J. (登録日: 2023-10-25, 公開日: 2024-04-03, 最終更新日: 2024-04-10)

主引用文献

Breeze, C.W.,Nakano, Y.,Campbell, E.C.,Frkic, R.L.,Lupton, D.W.,Jackson, C.J.
Mononuclear binding and catalytic activity of europium(III) and gadolinium(III) at the active site of the model metalloenzyme phosphotriesterase.
Acta Crystallogr D Struct Biol, 80:289-298, 2024

PubMed Abstract: Lanthanide ions have ideal chemical properties for catalysis, such as hard Lewis acidity, fast ligand-exchange kinetics, high coordination-number preferences and low geometric requirements for coordination. As a result, many small-molecule lanthanide catalysts have been described in the literature. Yet, despite the ability of enzymes to catalyse highly stereoselective reactions under gentle conditions, very few lanthanoenzymes have been investigated. In this work, the mononuclear binding of europium(III) and gadolinium(III) to the active site of a mutant of the model enzyme phosphotriesterase are described using X-ray crystallography at 1.78 and 1.61 Å resolution, respectively. It is also shown that despite coordinating a single non-natural metal cation, the PTE-R18 mutant is still able to maintain esterase activity.

PubMed: 38512071
DOI: 10.1107/S2059798324002316

実験手法

X-RAY DIFFRACTION (1.78 Å)