8xhy

The complex structure of mutant T307A of SsBcmE and its natural substrate cIL

spinqualitylabelsall models 8xhy, resolution 1.71Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8xhy is a 1 chain structure with sequence from Streptomyces cinnamoneus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7100197Å Ligands: A1LVH, AKG, FE2, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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)/alpha-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. Three distinct strategies lead to programmable aliphatic C-H oxidation in bicyclomycin biosynthesis.,Wu L, He JB, Wei W, Pan HX, Wang X, Yang S, Liang Y, Tang GL, Zhou J Nat Commun. 2025 May 19;16(1):4651. doi: 10.1038/s41467-025-58997-8. PMID:40389404 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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