title: The sequence of the enterococcal cytolysin imparts unusual lanthionine stereochemistry.
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.
authors: Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.
authors: Weixin
authors: W
authors: Tang
authors: Wilfred A
authors: WA
authors: van der Donk
mesh_terms: D000409:Alanine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D016983:Enterococcus / Q000737:chemistry*; D008968:Molecular Conformation; D054353:Perforin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D013237:Stereoisomerism; D013440:Sulfides / Q000737:chemistry* / Q000378:metabolism
chemical_list: D013440:Sulfides; D054353:Perforin; C001520:lanthionine; D000409:Alanine