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http://purl.uniprot.org/citations/15361862http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15361862http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15361862http://www.w3.org/2000/01/rdf-schema#comment"The emerging antibiotics-resistance problem has underlined the urgent need for novel antimicrobial agents. Lantibiotics (lanthionine-containing antibiotics) are promising candidates to alleviate this problem. Nisin, a member of this family, has a unique pore-forming activity against bacteria. It binds to lipid II, the essential precursor of cell wall synthesis. As a result, the membrane permeabilization activity of nisin is increased by three orders of magnitude. Here we report the solution structure of the complex of nisin and lipid II. The structure shows a novel lipid II-binding motif in which the pyrophosphate moiety of lipid II is primarily coordinated by the N-terminal backbone amides of nisin via intermolecular hydrogen bonds. This cage structure provides a rationale for the conservation of the lanthionine rings among several lipid II-binding lantibiotics. The structure of the pyrophosphate cage offers a template for structure-based design of novel antibiotics."xsd:string
http://purl.uniprot.org/citations/15361862http://purl.org/dc/terms/identifier"doi:10.1038/nsmb830"xsd:string
http://purl.uniprot.org/citations/15361862http://purl.org/dc/terms/identifier"doi:10.1038/nsmb830"xsd:string
http://purl.uniprot.org/citations/15361862http://purl.uniprot.org/core/author"van Nuland N.A."xsd:string
http://purl.uniprot.org/citations/15361862http://purl.uniprot.org/core/author"van Nuland N.A."xsd:string
http://purl.uniprot.org/citations/15361862http://purl.uniprot.org/core/author"Kaptein R."xsd:string
http://purl.uniprot.org/citations/15361862http://purl.uniprot.org/core/author"Kaptein R."xsd:string
http://purl.uniprot.org/citations/15361862http://purl.uniprot.org/core/author"Bonvin A.M."xsd:string
http://purl.uniprot.org/citations/15361862http://purl.uniprot.org/core/author"Bonvin A.M."xsd:string
http://purl.uniprot.org/citations/15361862http://purl.uniprot.org/core/author"Breukink E."xsd:string
http://purl.uniprot.org/citations/15361862http://purl.uniprot.org/core/author"Breukink E."xsd:string
http://purl.uniprot.org/citations/15361862http://purl.uniprot.org/core/author"de Kruijff B."xsd:string
http://purl.uniprot.org/citations/15361862http://purl.uniprot.org/core/author"de Kruijff B."xsd:string
http://purl.uniprot.org/citations/15361862http://purl.uniprot.org/core/author"Hsu S.T."xsd:string
http://purl.uniprot.org/citations/15361862http://purl.uniprot.org/core/author"Hsu S.T."xsd:string
http://purl.uniprot.org/citations/15361862http://purl.uniprot.org/core/author"Lutters M.A."xsd:string
http://purl.uniprot.org/citations/15361862http://purl.uniprot.org/core/author"Lutters M.A."xsd:string
http://purl.uniprot.org/citations/15361862http://purl.uniprot.org/core/author"Tischenko E."xsd:string
http://purl.uniprot.org/citations/15361862http://purl.uniprot.org/core/author"Tischenko E."xsd:string
http://purl.uniprot.org/citations/15361862http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15361862http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15361862http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/15361862http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string