The sequence of the enterococcal cytolysin imparts unusual lanthionine stereochemistry

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Abstract

The enterococcal cytolysin is a two-component lantibiotic of unknown structure with hemolytic activity that is important for virulence. We prepared cytolysin by coexpression of each precursor peptide with the synthetase CylM in Escherichia coli and characterized its structure. Unexpectedly, cytolysin is to our knowledge the first example of a lantibiotic containing lanthionine and methyllanthionine structures with different stereochemistries in the same peptide. The stereochemistry is determined by the sequence of the substrate peptide.

Original languageEnglish (US)
Pages (from-to)157-159
Number of pages3
JournalNature chemical biology
Volume9
Issue number3
DOIs
StatePublished - Mar 1 2013

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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