6L86
The structure of SfaA
Summary for 6L86
Entry DOI | 10.2210/pdb6l86/pdb |
Descriptor | Taurine catabolism dioxygenase, FE (II) ION, (2S)-2-hydroxybutanedioic acid, ... (5 entities in total) |
Functional Keywords | iron(ii) and 2-oxoglutarate dependent oxygenases, oxidoreductase |
Biological source | Streptomyces thioluteus |
Total number of polymer chains | 4 |
Total formula weight | 144541.95 |
Authors | Chen, T.Y.,Chen, J.,Zhou, J.,Chang, W. (deposition date: 2019-11-05, release date: 2020-03-04, Last modification date: 2023-11-22) |
Primary citation | Chen, T.Y.,Chen, J.,Tang, Y.,Zhou, J.,Guo, Y.,Chang, W.C. Pathway from N-Alkylglycine to Alkylisonitrile Catalyzed by Iron(II) and 2-Oxoglutarate-Dependent Oxygenases. Angew.Chem.Int.Ed.Engl., 59:7367-7371, 2020 Cited by PubMed Abstract: N-alkylisonitrile, a precursor to isonitrile-containing lipopeptides, is biosynthesized by decarboxylation-assisted -N≡C 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. Reported here is a plausible mechanism of three Fe/2OG enzymes, Sav607, ScoE and SfaA, which catalyze 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≡C bond formation involves two cycles of Fe/2OG enzyme catalysis. The reaction starts with an Fe -oxo-catalyzed hydroxylation. It is likely followed by decarboxylation-assisted desaturation to complete isonitrile installation. PubMed: 32074393DOI: 10.1002/anie.201914896 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.23 Å) |
Structure validation
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