title: Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis.
abstract: Nisin is a posttranslationally modified antimicrobial peptide that is widely used as a food preservative. It contains five cyclic thioethers of varying sizes that are installed by a single enzyme, NisC. Reported here are the in vitro reconstitution of the cyclization process and the x-ray crystal structure of the NisC enzyme. The structure reveals similarities in fold and substrate activation with mammalian farnesyl transferases, suggesting that human homologs of NisC posttranslationally modify a cysteine of a protein substrate.
authors.affiliation: Department of Biochemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA.
authors.forename: Bo
authors.initials: B
authors.lastname: Li
authors.forename: John Paul J
authors.initials: JP
authors.lastname: Yu
authors.forename: Joseph S
authors.initials: JS
authors.lastname: Brunzelle
authors.forename: Gert N
authors.initials: GN
authors.lastname: Moll
authors.forename: Wilfred A
authors.initials: WA
authors.lastname: van der Donk
authors.forename: Satish K
authors.initials: SK
authors.lastname: Nair
mesh_terms: D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000096:biosynthesis* / Q000737:chemistry; D013437:Carbon-Sulfur Lyases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D018360:Crystallography, X-Ray; D051231:Farnesyltranstransferase / Q000737:chemistry; D006801:Humans; D013294:Lactococcus lactis / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009561:Nisin / Q000096:biosynthesis* / Q000737:chemistry; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
chemical_list: D000900:Anti-Bacterial Agents; D009561:Nisin; D051231:Farnesyltranstransferase; D013437:Carbon-Sulfur Lyases