8Y4U
Crystal structure of a His1 from oryza sativa
Summary for 8Y4U
| Entry DOI | 10.2210/pdb8y4u/pdb |
| Descriptor | Fe(II)/2-oxoglutarate-dependent oxygenase, FE (III) ION (3 entities in total) |
| Functional Keywords | hppd inhibitor sensitive 1; oxygenase;, plant protein |
| Biological source | Oryza sativa subsp. japonica (Rice) |
| Total number of polymer chains | 1 |
| Total formula weight | 40224.29 |
| Authors | Wang, N.,Ma, J.M.,Shibing, H.,Beibei, Y.,He, Z.,Dandan, L. (deposition date: 2024-01-30, release date: 2024-02-28, Last modification date: 2024-04-03) |
| Primary citation | Wang, N.,He, S.,Yang, B.,Zhang, H.,Liu, D.,Song, P.,Chen, T.,Wang, W.,Ge, H.,Ma, J. Crystal structure of HPPD inhibitor sensitive protein from Oryza sativa. Biochem.Biophys.Res.Commun., 704:149672-149672, 2024 Cited by PubMed Abstract: 4-hydroxyphenylpyruvate dioxygenase (HPPD) Inhibitor Sensitive 1 (HIS1) is an endogenous gene of rice, conferring broad-spectrum resistance to β-triketone herbicides. Similar genes, known as HIS1-like genes (HSLs), exhibit analogous functions and can complement the herbicide-resistant characteristics endowed by HIS1. The identification of HIS1 and HSLs represents a valuable asset, as the intentional pairing of herbicides with resistance genes emerges as an effective strategy for crop breeding. Encoded by HIS1 is a Fe(II)/2-oxoglutarate-dependent oxygenase responsible for detoxifying β-triketone herbicides through hydroxylation. However, the precise structure supporting this function remains unclear. This work, which determined the crystal structure of HIS1, reveals a conserved core motif of Fe(II)/2-oxoglutarate-dependent oxygenase and pinpoints the crucial residue dictating substrate preference between HIS1 and HSL. PubMed: 38401306DOI: 10.1016/j.bbrc.2024.149672 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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