Structure and mechanism of lanthipeptide biosynthetic enzymes

Wilfred A. van der Donk; Satish K. Nair

doi:10.1016/j.sbi.2014.09.006

Structure and mechanism of lanthipeptide biosynthetic enzymes

Research output: Contribution to journal › Review article › peer-review

Abstract

Lanthipeptides are members of the ribosomally synthesized and post-translationally modified peptide (RiPP) natural products. They contain thioether crosslinks generated by dehydration of Ser and Thr residues followed by the addition of the thiol of Cys residues to the dehydroamino acids. Recent studies have revealed unexpected mechanisms of the post-translational modifications, and structural studies have started to provide insights into recognition of the peptide substrates by the modification enzymes.

Original language	English (US)
Pages (from-to)	58-66
Number of pages	9
Journal	Current Opinion in Structural Biology
Volume	29
DOIs	https://doi.org/10.1016/j.sbi.2014.09.006
State	Published - Dec 1 2014

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1016/j.sbi.2014.09.006

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AU - Nair, Satish K.

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AB - Lanthipeptides are members of the ribosomally synthesized and post-translationally modified peptide (RiPP) natural products. They contain thioether crosslinks generated by dehydration of Ser and Thr residues followed by the addition of the thiol of Cys residues to the dehydroamino acids. Recent studies have revealed unexpected mechanisms of the post-translational modifications, and structural studies have started to provide insights into recognition of the peptide substrates by the modification enzymes.

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Structure and mechanism of lanthipeptide biosynthetic enzymes

Abstract

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