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Biosynthesis

Leading the way to RiPPs

Nature Chemical Biology volume 11, pages 551–552 (2015)Cite this article

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Many peptide-based natural products require a leader peptide to reach their final modified form, but the identification of general rules for leader peptide interactions have been stymied by the diversity of these molecules. Two papers reporting crystallographic and bioinformatic analysis of these systems now reveal a structurally conserved domain that mediates leader peptide binding.

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Figure 1: Binding of diverse RiPP precursor peptides to their biosynthetic enzymes is mediated by a conserved domain related to the protein PqqD.

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  1. A. James Link is in the Departments of Chemical and Biological Engineering and Molecular Biology, Princeton University, Princeton, New Jersey, USA.,

    A James Link

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Correspondence to A James Link.

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Link, A. Leading the way to RiPPs. Nat Chem Biol 11, 551–552 (2015). https://doi.org/10.1038/nchembio.1862

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