8XHY
The complex structure of mutant T307A of SsBcmE and its natural substrate cIL
This is a non-PDB format compatible entry.
Summary for 8XHY
| Entry DOI | 10.2210/pdb8xhy/pdb |
| Descriptor | Fe/2OG dependent dioxygenase, FE (II) ION, 2-OXOGLUTARIC ACID, ... (6 entities in total) |
| Functional Keywords | c-h activation, selectivity, fe/2og dependent dioxygenase, oxidoreductase |
| Biological source | Streptomyces cinnamoneus |
| Total number of polymer chains | 1 |
| Total formula weight | 36900.70 |
| Authors | |
| Primary citation | Wu, L.,He, J.B.,Wei, W.,Pan, H.X.,Wang, X.,Yang, S.,Liang, Y.,Tang, G.L.,Zhou, J. Three distinct strategies lead to programmable aliphatic C-H oxidation in bicyclomycin biosynthesis. Nat Commun, 16:4651-4651, 2025 Cited by PubMed Abstract: The C-H bond functionalization has been widely used in chemical synthesis over the past decade. However, regio- and stereoselectivity still remain a significant challenge, especially for inert aliphatic C-H bonds. Here we report the mechanism of three Fe(II)/α-ketoglutarate-dependent dioxygenases in bicyclomycin synthesis, which depicts the natural tactic to sequentially hydroxylate specific C-H bonds of similar substrates (cyclodipeptides). Molecular basis by crystallographic studies, computational simulations, and site-directed mutagenesis reveals the exquisite arrangement of three enzymes using mutually orthogonal strategies to realize three different regio-selectivities. Moreover, this programmable selective hydroxylation can be extended to other cyclodipeptides. This evidence not only provides a naturally occurring showcase corresponding to the widely used methods in chemical catalysis but also expands the toolbox of biocatalysts to address the regioselective functionalization of C-H bonds. PubMed: 40389404DOI: 10.1038/s41467-025-58997-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.71001968611 Å) |
Structure validation
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