Report

Structure and Mechanism of the Lantibiotic Cyclase Involved in Nisin Biosynthesis

Science  10 Mar 2006:
Vol. 311, Issue 5766, pp. 1464-1467
DOI: 10.1126/science.1121422

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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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