8x7c
From Proteopedia
Crystal structure of ZmHSL1A
Structural highlights
FunctionPublication Abstract from PubMedDiscovering and engineering herbicide-resistant genes is a crucial challenge in crop breeding. This study focuses on the 4-hydroxyphenylpyruvate dioxygenase Inhibitor Sensitive 1-Like (HSL) protein, prevalent in higher plants and exhibiting weak catalytic activity against many beta-triketone herbicides (beta-THs). The crystal structures of maize HSL1A complexed with beta-THs were elucidated, identifying four essential herbicide-binding residues and explaining the weak activity of HSL1A against the herbicides. Utilizing an artificial evolution approach, we developed a series of rice HSL1 mutants targeting the four residues. Then, these mutants were systematically evaluated, identifying the M10 variant as the most effective in modifying beta-THs. The initial active conformation of substrate binding in HSL1 was also revealed from these mutants. Furthermore, overexpression of M10 in rice significantly enhanced resistance to beta-THs, resulting in a notable 32-fold increase in resistance to methyl-benquitrione. In conclusion, the artificially evolved M10 gene shows great potential for the development of herbicide-resistant crops. An artificially evolved gene for herbicide-resistant rice breeding.,Dong J, Yu XH, Dong J, Wang GH, Wang XL, Wang DW, Yan YC, Xiao H, Ye BQ, Lin HY, Yang GF Proc Natl Acad Sci U S A. 2024 Aug 20;121(34):e2407285121. doi: , 10.1073/pnas.2407285121. Epub 2024 Aug 12. PMID:39133859[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Large Structures | Zea mays | Dong J | Lin H-Y | Yang G-F