Crystal structures of herbicide-detoxifying esterase reveal a lid loop affecting substrate binding and activity
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 improv...
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2023-07-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-023-40103-5 |
| _version_ | 1797774096081092608 |
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| author | Bin Liu Weiwu Wang Jiguo Qiu Xing Huang Shenshen Qiu Yixuan Bao Siqiong Xu Luyao Ruan Tingting Ran Jian He |
| author_facet | Bin Liu Weiwu Wang Jiguo Qiu Xing Huang Shenshen Qiu Yixuan Bao Siqiong Xu Luyao Ruan Tingting Ran Jian He |
| author_sort | Bin Liu |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-12T22:16:04Z |
| format | Article |
| id | doaj.art-8b13e35d3d53443dbba2024a2b16aa05 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-03-12T22:16:04Z |
| publishDate | 2023-07-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-8b13e35d3d53443dbba2024a2b16aa052023-07-23T11:19:10ZengNature PortfolioNature Communications2041-17232023-07-0114111210.1038/s41467-023-40103-5Crystal structures of herbicide-detoxifying esterase reveal a lid loop affecting substrate binding and activityBin Liu0Weiwu Wang1Jiguo Qiu2Xing Huang3Shenshen Qiu4Yixuan Bao5Siqiong Xu6Luyao Ruan7Tingting Ran8Jian He9Key Laboratory of Agricultural Environmental Microbiology of Ministry of Agriculture, College of Life Sciences, Nanjing Agricultural UniversityKey Laboratory of Agricultural Environmental Microbiology of Ministry of Agriculture, College of Life Sciences, Nanjing Agricultural UniversityKey Laboratory of Agricultural Environmental Microbiology of Ministry of Agriculture, College of Life Sciences, Nanjing Agricultural UniversityKey Laboratory of Agricultural Environmental Microbiology of Ministry of Agriculture, College of Life Sciences, Nanjing Agricultural UniversityKey Laboratory of Agricultural Environmental Microbiology of Ministry of Agriculture, College of Life Sciences, Nanjing Agricultural UniversityKey Laboratory of Agricultural Environmental Microbiology of Ministry of Agriculture, College of Life Sciences, Nanjing Agricultural UniversityKey Laboratory of Agricultural Environmental Microbiology of Ministry of Agriculture, College of Life Sciences, Nanjing Agricultural UniversityKey Laboratory of Agricultural Environmental Microbiology of Ministry of Agriculture, College of Life Sciences, Nanjing Agricultural UniversityKey Laboratory of Agricultural Environmental Microbiology of Ministry of Agriculture, College of Life Sciences, Nanjing Agricultural UniversityKey Laboratory of Agricultural Environmental Microbiology of Ministry of Agriculture, College of Life Sciences, Nanjing Agricultural UniversityAbstract 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.https://doi.org/10.1038/s41467-023-40103-5 |
| spellingShingle | Bin Liu Weiwu Wang Jiguo Qiu Xing Huang Shenshen Qiu Yixuan Bao Siqiong Xu Luyao Ruan Tingting Ran Jian He Crystal structures of herbicide-detoxifying esterase reveal a lid loop affecting substrate binding and activity Nature Communications |
| title | Crystal structures of herbicide-detoxifying esterase reveal a lid loop affecting substrate binding and activity |
| title_full | Crystal structures of herbicide-detoxifying esterase reveal a lid loop affecting substrate binding and activity |
| title_fullStr | Crystal structures of herbicide-detoxifying esterase reveal a lid loop affecting substrate binding and activity |
| title_full_unstemmed | Crystal structures of herbicide-detoxifying esterase reveal a lid loop affecting substrate binding and activity |
| title_short | Crystal structures of herbicide-detoxifying esterase reveal a lid loop affecting substrate binding and activity |
| title_sort | crystal structures of herbicide detoxifying esterase reveal a lid loop affecting substrate binding and activity |
| url | https://doi.org/10.1038/s41467-023-40103-5 |
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