8IW3

crystal structure of SulE mutant

Summary for 8IW3

• Entry DOI: 10.2210/pdb8iw3/pdb
• Descriptor: Alpha/beta fold hydrolase, 2-[[[[(4-CHLORO-6-METHOXY-2-PYRIMIDINYL)AMINO]CARBONYL]AMINO]SULFONYL]BENZOIC ACID ETHYL ESTER, L(+)-TARTARIC ACID, ... (5 entities in total)
• Functional Keywords: complex, sule, mutant, hydrolase
• Biological source: Hansschlegelia zhihuaiae
• Total number of polymer chains: 2
• Total formula weight: 83498.47

Authors

Liu, B.,He, J.,Ran, T.,Wang, W. (deposition date: 2023-03-29, release date: 2023-08-02, Last modification date: 2024-05-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.56 Å)