9KGM
Complex structure of OsHPPD with MBQ
Summary for 9KGM
| Entry DOI | 10.2210/pdb9kgm/pdb |
| Descriptor | 4-hydroxyphenylpyruvate dioxygenase, COBALT (II) ION, 1,5-dimethyl-3-(2-methylphenyl)-6-(2-oxidanyl-6-oxidanylidene-cyclohexen-1-yl)carbonyl-quinazoline-2,4-dione (3 entities in total) |
| Functional Keywords | inhibitor, complex, hppd, oxidoreductase |
| Biological source | Oryza sativa subsp. japonica (rice) |
| Total number of polymer chains | 2 |
| Total formula weight | 94933.23 |
| Authors | Yang, G.-F.,Lin, H.-Y.,Dong, J. (deposition date: 2024-11-08, release date: 2025-11-12, Last modification date: 2026-04-22) |
| Primary citation | Dong, J.,Dong, J.,Wang, X.L.,Wei, X.F.,Yang, G.F.,Lin, H.Y. Structure-Based Directed Evolution of Rice 4-Hydroxyphenylpyruvate Dioxygenase Confers Enhanced Herbicide Tolerance. J.Agric.Food Chem., 73:18923-18931, 2025 Cited by PubMed Abstract: Precise gene modification is pivotal in molecular breeding. 4-Hydroxyphenylpyruvate dioxygenase (HPPD) plays a crucial role in the development of herbicide-resistant crops. But how to modify HPPD and thereby confer herbicide resistance in plants remains unclear. This research delineates the structure of HPPD (HPPD) complexed with Methyl-Benquitrione (MBQ) and identifies potential residues that confer herbicide resistance. Enzymatic tests of the C-terminal α9 helix variants showed that K418D, E423Q, E423M, E423S, E423T, E423L, E423W, E432I, E432M, E432W, and E432F demonstrated preserved catalytic efficiency. The herbicide resistance test displayed that K418D, E423Q, E423M, E432I, and E432M acquired 1.5- to 3-fold enhancements against mesotrione, topramezone, MBQ, and A1 in vitro. Especially, the forced expression of E432M in significantly elevated herbicide resistance compared to the wild type. These findings highlight the potential of specific HPPD modifications in developing crops with enhanced herbicide resistance, providing a foundation for future genetic engineering strategies. PubMed: 40668751DOI: 10.1021/acs.jafc.5c06678 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.89 Å) |
Structure validation
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