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Structure–Activity Relationships of the S‑Linked Glycocin Sublancin

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journal contribution
posted on 07.11.2017, 00:00 by Subhanip Biswas, Chantal V. Garcia De Gonzalo, Lindsay M. Repka, Wilfred A. van der Donk
Sublancin is a 37-amino acid antimicrobial peptide belonging to the glycocin family of natural products. It contains two helices that are held together by two disulfide bonds as well as an unusual S-glucosidic linkage to a Cys in a loop connecting the helices. We report the reconstitution of the biosynthetic pathway to this natural product in Escherichia coli. This technology enabled the evaluation of the structure–activity relationships of the solvent-exposed residues in the helices. The biosynthetic machinery proved tolerant of changes in both helices, and the bioactivity studies of the resulting mutants show that two residues in helix B are important for bioactivity, Asn31 and Arg33.

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