8IVE

crystal structure of SulE mutant

8IVE の概要

• エントリーDOI: 10.2210/pdb8ive/pdb
• 分子名称: Alpha/beta fold hydrolase, 2-[[[[(4-CHLORO-6-METHOXY-2-PYRIMIDINYL)AMINO]CARBONYL]AMINO]SULFONYL]BENZOIC ACID ETHYL ESTER, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: complex, sule, mutant, hydrolase
• 由来する生物種: Hansschlegelia zhihuaiae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 83318.45

構造登録者

Liu, B.,He, J.,Ran, T.,Wang, W. (登録日: 2023-03-27, 公開日: 2023-08-02, 最終更新日: 2024-05-29)

主引用文献

Liu, B.,Wang, W.,Qiu, J.,Huang, X.,Qiu, S.,Bao, Y.,Xu, S.,Ruan, L.,Ran, T.,He, J.
Crystal structures of herbicide-detoxifying esterase reveal a lid loop affecting substrate binding and activity.
Nat Commun, 14:4343-4343, 2023

PubMed Abstract: SulE, an esterase, which detoxifies a variety of sulfonylurea herbicides through de-esterification, provides an attractive approach to remove environmental sulfonylurea herbicides and develop herbicide-tolerant crops. Here, we determined the crystal structures of SulE and an activity improved mutant P44R. Structural analysis revealed that SulE is a dimer with spacious binding pocket accommodating the large sulfonylureas substrate. Particularly, SulE contains a protruding β hairpin with a lid loop covering the active site of the other subunit of the dimer. The lid loop participates in substrate recognition and binding. P44R mutation altered the lid loop flexibility, resulting in the sulfonylurea heterocyclic ring repositioning to a relative stable conformation thus leading to dramatically increased activity. Our work provides important insights into the molecular mechanism of SulE, and establish a solid foundation for further improving the enzyme activity to various sulfonylurea herbicides through rational design.

PubMed: 37468532
DOI: 10.1038/s41467-023-40103-5

実験手法

X-RAY DIFFRACTION (1.44 Å)