6DCH

Structure of isonitrile biosynthesis enzyme ScoE

Summary for 6DCH

• Entry DOI: 10.2210/pdb6dch/pdb
• Descriptor: ScoE protein, ACETATE ION, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: isonitrile, non-heme iron, enzyme, metalloenzyme, oxidoreductase
• Biological source: Streptomyces coeruleorubidus
• Total number of polymer chains: 1
• Total formula weight: 37146.39

Authors

Born, D.A.,Drennan, C.L. (deposition date: 2018-05-07, release date: 2018-06-27, Last modification date: 2023-10-11)

Primary citation

Harris, N.C.,Born, D.A.,Cai, W.,Huang, Y.,Martin, J.,Khalaf, R.,Drennan, C.L.,Zhang, W.
Isonitrile Formation by a Non-Heme Iron(II)-Dependent Oxidase/Decarboxylase.
Angew. Chem. Int. Ed. Engl., 57:9707-9710, 2018

PubMed Abstract: The electron-rich isonitrile is an important functionality in bioactive natural products, but its biosynthesis has been restricted to the IsnA family of isonitrile synthases. We herein provide the first structural and biochemical evidence of an alternative mechanism for isonitrile formation. ScoE, a putative non-heme iron(II)-dependent enzyme from Streptomyces coeruleorubidus, was shown to catalyze the conversion of (R)-3-((carboxymethyl)amino)butanoic acid to (R)-3-isocyanobutanoic acid through an oxidative decarboxylation mechanism. This work further provides a revised scheme for the biosynthesis of a unique class of isonitrile lipopeptides, of which several members are critical for the virulence of pathogenic mycobacteria.

PubMed: 29906336
DOI: 10.1002/anie.201804307

Experimental method

X-RAY DIFFRACTION (1.8 Å)