EC Number   |
|---|
    1.13.11.27 | a ligand-mediated conformational switch in helix H11 mediates rapid substrate access followed by active site closing and efficient product release through H11 opening. In mutant HPPD, large differences in H11 gating are found with correlation to experimentally measured herbicide tolerance |
| 1.13.11.27 | comparison of Arabidopsis thaiana and human enzyme. In human, the carboxyl group of substrate 4-hydroxyphenylpyruvate interacts by a H-bond network formed by Gln334, metal-binding ligand Glu349, and Asn363 in the C-terminal helix. The 4-hydroxyl group of the substrate interacts with Gln251 and Gln265 |
| 1.13.11.27 | crystal structure analysis of HPPD-Fe(II)-acetate complex, PDB ID 1CJX |
| 1.13.11.27 | crystal structure at 2.4 A resolution |
| 1.13.11.27 | crystals are grown by sitting-drop vapor diffusion method at 20°C |
| 1.13.11.27 | Fe(II)-form in complex with inhibitor 2-[2-nitro-4-(trifluoromethyl)benzoyl]-1,3-cyclohexanedione |
| 1.13.11.27 | hanging-drop method in 18-25% PEG 4000, 0.2 M ammonium acetate, 0.1 M trisodium citrate, pH 5.6, at room temperature |
| 1.13.11.27 | homology modeling of structure and docking of inhibitors. Each molecule consists of 9 alpha-helices and 2 twisted barrel-like beta-sheets, and the active site is located at the C-terminus |
| 1.13.11.27 | structure in complex with inhibitor 2-benzyl-5-(5-hydroxy-1-methyl-1H-pyrazole-4-carbonyl)-1H-isoindole-1,3(2H)-dione at a resolution of 1.8 A. The two carbonyl groups of 2-benzoylethen-1-ol formed a bidentate chelating interaction with the metal ion, while the isoindoline-1,3-dione moiety formes pronounced pi-pi stacking interactions with Phe381 and Phe424 |
| 1.13.11.27 | structure of HPPD in complex with substrate 4-hydroxyphenylpyruvate at a resolution of 2.80 A. 4-Hydroxyphenylpyruvate takes keto rather than enol form inside the HPPD active pocket. Residues Phe424, Asn423, Glu394, Gln307, Asn282, and Ser267 play important roles in substrate binding and catalytic cycle. Residue Gln293 undergoes a rotation upon the HPPA binding and forms H-bond network of Ser267-Asn282-Gln307-Gln293, resulting in the transformation of HPPD from an inactive state to active state |
