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

Research output: Contribution to journalArticle

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

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