8YZN

Crystal structural analysis of PaL

「8JJ7」から置き換えられました

8YZN の概要

• エントリーDOI: 10.2210/pdb8yzn/pdb
• 分子名称: Lipase (2 entities in total)
• 機能のキーワード: lipase, pseudomonas alcaligenes, l-menthol, biosynthetic protein
• 由来する生物種: Pseudomonas alcaligenes
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52821.14

構造登録者

Xu, G.,Wu, J. (登録日: 2024-04-07, 公開日: 2024-04-17, 最終更新日: 2024-10-30)

主引用文献

Xu, G.,Guo, H.,Yu, Z.,Wang, S.,Shen, D.,Yang, L.,Wu, J.,Chen, B.,Yu, H.
Crystal structure of lipase from Pseudomonas aeruginosa reveals an unusual catalytic triad conformation.
Structure, 32:1454-1464.e3, 2024

PubMed Abstract: The Pseudomonas aeruginosa lipase PaL catalyzes the stereoselective hydrolysis of menthyl propionate to produce L-menthol. The lack of a three-dimensional structure of PaL has so far prevented a detailed understanding of its stereoselective reaction mechanism. Here, the crystal structure of PaL was determined at a resolution of 1.80 Å by single-wavelength anomalous diffraction. In the apo-PaL structure, the catalytic His302 is located in a long loop on the surface that is solvent exposed. His302 is distant from the other two catalytic residues, Asp274 and Ser164. This configuration of catalytic residues is unusual for lipases. Using metadynamics simulations, we observed that the enzyme undergoes a significant conformational change upon ligand binding. We also explored the catalytic and stereoselectivity mechanisms of PaL by all-atom molecular dynamics simulations. These findings could guide the engineering of PaL with an improved diastereoselectivity for L-menthol production.

PubMed: 39025068
DOI: 10.1016/j.str.2024.06.014

実験手法

X-RAY DIFFRACTION (1.799 Å)