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6L86

The structure of SfaA

Summary for 6L86
Entry DOI10.2210/pdb6l86/pdb
DescriptorTaurine catabolism dioxygenase, FE (II) ION, (2S)-2-hydroxybutanedioic acid, ... (5 entities in total)
Functional Keywordsiron(ii) and 2-oxoglutarate dependent oxygenases, oxidoreductase
Biological sourceStreptomyces thioluteus
Total number of polymer chains4
Total formula weight144541.95
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 citationChen, 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: 32074393
DOI: 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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