6dch

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Structure of isonitrile biosynthesis enzyme ScoEStructure of isonitrile biosynthesis enzyme ScoE

Structural highlights

6dch is a 1 chain structure with sequence from Streptomyces coeruleorubidus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A3B6UEU3_STRC4

Publication Abstract from PubMed

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 here 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, members of which are critical for the virulence of pathogenic mycobacteria.

Isonitrile Formation by a Non-heme Iron(II)-Dependent Oxidase/Decarboxylase.,Harris N, Born D, Cai W, Huang Y, Martin J, Khalaf R, Drennan C, Zhang W Angew Chem Int Ed Engl. 2018 Jun 15. doi: 10.1002/anie.201804307. PMID:29906336[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Harris N, Born D, Cai W, Huang Y, Martin J, Khalaf R, Drennan C, Zhang W. Isonitrile Formation by a Non-heme Iron(II)-Dependent Oxidase/Decarboxylase. Angew Chem Int Ed Engl. 2018 Jun 15. doi: 10.1002/anie.201804307. PMID:29906336 doi:http://dx.doi.org/10.1002/anie.201804307

6dch, resolution 1.80Å

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OCA