6vgt | pdb_00006vgt

Solution NMR structure of enterococcal cytolysin L (CylLL") produced by Enterococcus faecalis

spinqualitylabelsall models 6vgt, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6vgt is a 1 chain structure with sequence from "enterococcus_proteiformis"_thiercelin_and_jouhaud_1903 "enterococcus proteiformis" thiercelin and jouhaud 1903. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: ABA, DAL, DBU, DHA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytolysin 3D structures

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