8X6Q
Crystal structure of OsHSL1 L204F/F298L/I335F complexed with 2-acetyl-cyclohexane-2,4-dione
Summary for 8X6Q
| Entry DOI | 10.2210/pdb8x6q/pdb |
| Descriptor | HPPD Inhibitor Sensitive 1-like 1 protein, 2-ethanoyl-3-oxidanyl-cyclohex-2-en-1-one, COBALT (II) ION, ... (5 entities in total) |
| Functional Keywords | complex, substrate, oxidoreductase |
| Biological source | Oryza sativa (Asian cultivated rice) |
| Total number of polymer chains | 4 |
| Total formula weight | 160696.38 |
| Authors | |
| Primary citation | Dong, J.,Yu, X.H.,Dong, J.,Wang, G.H.,Wang, X.L.,Wang, D.W.,Yan, Y.C.,Xiao, H.,Ye, B.Q.,Lin, H.Y.,Yang, G.F. An artificially evolved gene for herbicide-resistant rice breeding. Proc.Natl.Acad.Sci.USA, 121:e2407285121-e2407285121, 2024 Cited by PubMed Abstract: Discovering 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 β-triketone herbicides (β-THs). The crystal structures of maize HSL1A complexed with β-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 β-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 β-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. PubMed: 39133859DOI: 10.1073/pnas.2407285121 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.39 Å) |
Structure validation
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