Crystal structures of herbicide-detoxifying esterase reveal a lid loop affecting substrate binding and activity.

doi:10.1038/s41467-023-40103-5

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Article

Crystal structures of herbicide-detoxifying esterase reveal a lid loop affecting substrate binding and activity.

Nature communications - 19 Jul 2023

Liu Bin, Wang Weiwu, Qiu Jiguo, Huang Xing, Qiu Shenshen, Bao Yixuan, Xu Siqiong, Ruan Luyao, Ran Tingting, He Jian

Abstract excerpt

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...

Topics

Esterases
Herbicides
Sulfonylurea Compounds
Catalytic Domain
Mutation
Binding Sites

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Identifiers

PMID: 37468532
DOI: 10.1038/s41467-023-40103-5
PMCID: PMC10356948

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