7y0l | pdb_00007y0l

SulE-S209A

spinqualitylabelsall models 7y0l, resolution 1.29Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7y0l is a 2 chain structure with sequence from Hansschlegelia zhihuaiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.29Å Ligands: 1MM, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G9I933_9HYPH Publication Abstract from PubMed 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 beta 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. Crystal structures of herbicide-detoxifying esterase reveal a lid loop affecting substrate binding and activity.,Liu B, Wang W, Qiu J, Huang X, Qiu S, Bao Y, Xu S, Ruan L, Ran T, He J Nat Commun. 2023 Jul 19;14(1):4343. doi: 10.1038/s41467-023-40103-5. PMID:37468532 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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