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. 2006 Mar 10;311(5766):1464-7.
doi: 10.1126/science.1121422.

Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis

Bo Li  1 , John Paul J Yu, Joseph S Brunzelle, Gert N Moll, Wilfred A van der Donk, Satish K Nair
Affiliations

Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis

Bo Li et al. Science. .

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.

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Comment in

  • Biochemistry. Five golden rings.
    Christianson DW. Christianson DW. Science. 2006 Mar 10;311(5766):1382-3. doi: 10.1126/science.1125298. Science. 2006. PMID: 16527957 No abstract available.

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