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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Autores principales: Tang, Weixin, van der Donk, Wilfred A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2013
Materias:
Article
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
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author Tang, Weixin
van der Donk, Wilfred A.
author_facet Tang, Weixin
van der Donk, Wilfred A.
author_sort Tang, Weixin
collection PubMed
description 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.
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spelling pubmed-35780372013-09-01 The Sequence of the Enterococcal Cytolysin Imparts Unusual Lanthionine Stereochemistry Tang, Weixin van der Donk, Wilfred A. Nat Chem Biol Article 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. 2013-01-13 2013-03 /pmc/articles/PMC3578037/ /pubmed/23314913 http://dx.doi.org/10.1038/nchembio.1162 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Tang, Weixin
van der Donk, Wilfred A.
The Sequence of the Enterococcal Cytolysin Imparts Unusual Lanthionine Stereochemistry
title The Sequence of the Enterococcal Cytolysin Imparts Unusual Lanthionine Stereochemistry
title_full The Sequence of the Enterococcal Cytolysin Imparts Unusual Lanthionine Stereochemistry
title_fullStr The Sequence of the Enterococcal Cytolysin Imparts Unusual Lanthionine Stereochemistry
title_full_unstemmed The Sequence of the Enterococcal Cytolysin Imparts Unusual Lanthionine Stereochemistry
title_short The Sequence of the Enterococcal Cytolysin Imparts Unusual Lanthionine Stereochemistry
title_sort sequence of the enterococcal cytolysin imparts unusual lanthionine stereochemistry
topic Article
url 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
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