9UAH
Crystal structure of the OkaE-W79A mutant with a-ketoglutarate and okaramine A
This is a non-PDB format compatible entry.
Summary for 9UAH
| Entry DOI | 10.2210/pdb9uah/pdb |
| Descriptor | Iron/alpha-ketoglutarate-dependent dioxygenase okaE, COBALT (II) ION, 2-OXOGLUTARIC ACID, ... (5 entities in total) |
| Functional Keywords | dioxygenase, non-heme, iron dependent, oxidoreductase |
| Biological source | Penicillium simplicissimum |
| Total number of polymer chains | 4 |
| Total formula weight | 142877.68 |
| Authors | |
| Primary citation | Wang, X.,Yu, J.,Liu, T.,Zhang, X.,Ju, M.,Xie, Z.,Naowarojna, N.,Ping, L.,Dong, Y.,Gong, B.,Xie, Y.,Nie, Y.,Hsiang, T.,Wu, R.,Zhang, L.,Liu, P.,Zhu, G.,Yan, W.,Liu, X. Structural and mechanistic insights into azetidine-associated alpha KG-NHFe enzyme OkaE with multifunctional catalysis. Nat Commun, 2026 Cited by PubMed Abstract: α-Ketoglutarate-dependent mononuclear non-haem iron (αKG-NHFe) enzymes are catalytically versatile, yet OkaE is unique for synthesizing azetidine rings via C-C bond formation. Here, we report the unexpected multifunctionality of OkaE, which catalyzes sequential oxidations. Isotopic labelling studies demonstrate that a second O₂ molecule participates in sequential epoxidation and ring cleavage, incorporating two oxygen atoms within a single catalytic cycle to form the previously unknown structure, neuokaramine IV. Crystal structures of the OkaE•Co•αKG•okaramine A complex unveil a unique methionine-π interaction network that facilitates substrate binding. Mutational and crystallographic analyses suggest this network fine-tunes substrate orientation relative to the metallo-centre, activating distinct reaction pathways at the 3a-OH or C8a positions. QM/MM simulations indicate that dynamic rotation of the Fe=O species initiates the cycle, enabling reaction bifurcation. This study elucidates the structural and mechanistic basis of OkaE's reactivity, highlighting its potential as a programmable biocatalyst for natural product diversification. PubMed: 41702921DOI: 10.1038/s41467-026-69519-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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