Structural highlights
Publication Abstract from PubMed
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.
The sequence of the enterococcal cytolysin imparts unusual lanthionine stereochemistry.,Tang W, van der Donk WA Nat Chem Biol. 2013 Mar;9(3):157-9. doi: 10.1038/nchembio.1162. Epub 2013 Jan 13. PMID:23314913[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tang W, van der Donk WA. The sequence of the enterococcal cytolysin imparts unusual lanthionine stereochemistry. Nat Chem Biol. 2013 Mar;9(3):157-9. doi: 10.1038/nchembio.1162. Epub 2013 Jan 13. PMID:23314913 doi:http://dx.doi.org/10.1038/nchembio.1162
