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Nature Research, Nature Chemical Biology, 3(9), p. 157-159, 2013

DOI: 10.1038/nchembio.1162

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The Sequence of the Enterococcal Cytolysin Imparts Unusual Lanthionine Stereochemistry

Journal article published in 2013 by Weixin Tang, Wilfred A. van der Donk ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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.