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The Sequence of the Enterococcal Cytolysin Imparts Unusual Lanthionine Stereochemistry

The enterococcal cytolysin is a two-component lantibiotic of unknown structure with hemolytic activity that is important for virulence. We prepared cytolysin by co-expression of each precursor peptide with the synthetase CylM in E. coli, and characterized its structure. Surprisingly, cytolysin is th...

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Detalles Bibliográficos
Autores principales: Tang, Weixin, van der Donk, Wilfred A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3578037/
https://www.ncbi.nlm.nih.gov/pubmed/23314913
http://dx.doi.org/10.1038/nchembio.1162
Descripción
Sumario:The enterococcal cytolysin is a two-component lantibiotic of unknown structure with hemolytic activity that is important for virulence. We prepared cytolysin by co-expression of each precursor peptide with the synthetase CylM in E. coli, and characterized its structure. Surprisingly, cytolysin is the first example of a lantibiotic containing lanthionine and methyllanthionine structures with different stereochemistries in the same peptide, which is determined by the sequence of the substrate peptide.