6l6w | pdb_00006l6w

The structure of ScoE with intermediate

spinqualitylabelsall models 6l6w, resolution 2.17Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6l6w is a 1 chain structure with sequence from "actinomyces_coeruleorubidus"_preobrazhenskaya_in_gauze_et_al._1957 "actinomyces coeruleorubidus" preobrazhenskaya in gauze et al. 1957. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: E79, FE2, FMT Gene: ScoE ("Actinomyces coeruleorubidus" Preobrazhenskaya in Gauze et al. 1957) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed N-alkylisonitrile, a precursor to isonitrile-containing lipopeptides, is biosynthesized via decarboxylation-assisted -N identical withC group (isonitrile) formation by using N-alkylglycine as the substrate. This reaction is catalyzed by iron(II) and 2-oxoglutarate (Fe/2OG) dependent enzymes. Distinct from typical oxygenation or halogenation reactions catalyzed by this class of enzymes, installation of the isonitrile group represents a novel reaction type for Fe/2OG enzymes that involves a four-electron oxidative process. Here we report the plausible mechanism of three Fe/2OG enzymes, Sav607, ScoE and SfaA, catalyzed isonitrile formation. The X-ray structures of iron loaded ScoE in complex with its substrate and the intermediate, along with biochemical and biophysical data reveal that -N identical withC bond formation involves two cycles of Fe/2OG enzyme catalysis. The reaction starts with an Fe(IV)-oxo catalyzed hydroxylation. It is likely followed by decarboxylation-assisted desaturation to complete isonitrile installation. Pathway from N-alkylglycine to alkylisonitrile catalyzed by iron(II) and 2-oxoglutarate dependent oxygenases.,Chang WC, Chen TY, Chen J, Tang Y, Zhou J, Guo Y Angew Chem Int Ed Engl. 2020 Feb 19. doi: 10.1002/anie.201914896. PMID:32074393 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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