9J1H
The binary complex structure of F2Y224-FtmOx1 mutant with alpha-ketoglutarate
Summary for 9J1H
| Entry DOI | 10.2210/pdb9j1h/pdb |
| Descriptor | Verruculogen synthase, COBALT (II) ION, 2-OXOGLUTARIC ACID, ... (6 entities in total) |
| Functional Keywords | dioxygenase, non-heme, iron dependent, oxidoreductase |
| Biological source | Aspergillus fumigatus Af293 (Neosartorya fumigata) |
| Total number of polymer chains | 2 |
| Total formula weight | 70834.23 |
| Authors | |
| Primary citation | Wang, X.,Yang, L.,Wang, S.,Wang, J.,Li, K.,Naowarojna, N.,Ju, Y.,Ye, K.,Han, Y.,Yan, W.,Liu, X.,Zhang, L.,Liu, P. Characterizing Y224 conformational flexibility in FtmOx1-catalysis using 19 F NMR spectroscopy. Catalysis Science And Technology, 15:386-395, 2025 Cited by PubMed Abstract: α-Ketoglutarate-dependent non-haem iron (αKG-NHFe) enzymes play a crucial role in natural product biosynthesis, and in some cases exhibiting multifunctional catalysis capability. This study focuses on αKG-NHFe enzyme FtmOx1, which catalyzes endoperoxidation, dealkylation, and alcohol oxidation reactions in verruculogen biosynthesis. We explore the hypothesis that the conformational dynamics of the active site Y224 confer the multifunctional activities of FtmOx1-catalysis. Utilizing Y224-to-3,5-difluorotyrosine-substituted FtmOx1, produced the amber codon suppression method, we conducted F NMR characterization to investigate FtmOx1's structural flexibility. Subsequent biochemical and X-ray crystallographic analyses provided insights into how specific conformations of FtmOx1-substrate complexes influence their catalytic activities. These findings underscore the utility of F NMR as a powerful tool for elucidating the complex mechanisms of multifunctional enzymes, offering potential avenues for developing biocatalytic processes to produce novel therapeutic agents harnessing their unique catalytic properties. PubMed: 39669701DOI: 10.1039/d4cy01077a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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