title: Structure and mechanism of lanthipeptide biosynthetic enzymes.
abstract: Lanthipeptides are members of the ribosomally synthesized and post-translationally modified peptide (RiPP) natural products. They contain thioether crosslinks generated by dehydration of Ser and Thr residues followed by the addition of the thiol of Cys residues to the dehydroamino acids. Recent studies have revealed unexpected mechanisms of the post-translational modifications, and structural studies have started to provide insights into recognition of the peptide substrates by the modification enzymes.
authors.affiliation: Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA; Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA; The Howard Hughes Medical Institute, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA. Electronic address: vddonk@illinois.edu.
authors.forename: Wilfred A
authors.initials: WA
authors.lastname: van der Donk
authors.affiliation: Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA; Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA. Electronic address: s-nair@life.uiuc.edu.
authors.forename: Satish K
authors.initials: SK
authors.lastname: Nair
mesh_terms: D000900:Anti-Bacterial Agents / Q000096:biosynthesis / Q000737:chemistry; D001419:Bacteria / Q000378:metabolism; D001430:Bacteriocins / Q000096:biosynthesis* / Q000737:chemistry*; D006836:Hydro-Lyases / Q000737:chemistry; D010088:Oxidoreductases / Q000737:chemistry; D010447:Peptide Hydrolases / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D012270:Ribosomes / Q000378:metabolism
chemical_list: D000900:Anti-Bacterial Agents; D001430:Bacteriocins; D010455:Peptides; C500288:epilancin 15X; D010088:Oxidoreductases; D010447:Peptide Hydrolases; D006836:Hydro-Lyases