Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis.

@article{Li2006StructureAM,
  title={Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis.},
  author={Bo Li and John Paul J Yu and Joseph S. Brunzelle and Gert N. Moll and Wilfred A van der Donk and Satish K Nair},
  journal={Science},
  year={2006},
  volume={311 5766},
  pages={
          1464-7
        }
}
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… CONTINUE READING
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