Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis

Bo Li, John Paul J Yu, Joseph S. Brunzelle, Gert N. Moll, Wilfred A. Van Der Donk*, Satish K. Nair

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

206 Scopus citations

Abstract

Nisin is a posttranslationally modified antimicrobial peptide that is widely used as a food preservative. It contains five cyclic thioethers of varying sizes that are installed by a single enzyme, NisC. Reported here are the in vitro reconstitution of the cyclization process and the x-ray crystal structure of the NisC enzyme. The structure reveals similarities in fold and substrate activation with mammalian farnesyl transferases, suggesting that human homologs of NisC posttranslationally modify a cysteine of a protein substrate.

Original languageEnglish (US)
Pages (from-to)1464-1467
Number of pages4
JournalScience
Volume311
Issue number5766
DOIs
StatePublished - Mar 10 2006

ASJC Scopus subject areas

  • General

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