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.
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Acknowledgements
We thank X. Yang (University of Illinois) for providing the modified HalA2 and Halβ peptides. This work was supported by the US National Institutes of Health (GM58822).
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W.T. and W.A.v.d.D. designed the study. W.T. performed all experiments. W.T. and W.A.v.d.D. analyzed the data and wrote the manuscript.
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Tang, W., van der Donk, W. The sequence of the enterococcal cytolysin imparts unusual lanthionine stereochemistry. Nat Chem Biol 9, 157–159 (2013). https://doi.org/10.1038/nchembio.1162
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DOI: https://doi.org/10.1038/nchembio.1162
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