Summary for 1WCO
| Entry DOI | 10.2210/pdb1wco/pdb |
| Related | 1AJ1 1MQX 1MQY 1MQZ 1QOW 1W9N 2DDE 2KTN 2KTO |
| Related PRD ID | PRD_000200 |
| Descriptor | ALA-FGA-LYS-DAL-DAL PEPTIDE, Lantibiotic, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-N-acetyl-alpha-muramic acid, ... (4 entities in total) |
| Functional Keywords | peptide-antibiotic complex, lantibiotic, antimicrobial, bacteriocin, thioester, pore formation, pyrophosphate cage, food preservative, peptide/antibiotic |
| Biological source | MONARTHROPALPUS FLAVUS More |
| Total number of polymer chains | 2 |
| Total formula weight | 4749.46 |
| Authors | Hsu, S.-T.D.,Breukink, E.,Tischenko, E.,Lutters, M.A.G.,de Kruijff, B.,Kaptein, R.,Bonvin, A.M.J.J.,van Nuland, N.A.J. (deposition date: 2004-11-19, release date: 2005-03-07, Last modification date: 2024-05-01) |
| Primary citation | Hsu, S.T.,Breukink, E.,Tischenko, E.,Lutters, M.A.,de Kruijff, B.,Kaptein, R.,Bonvin, A.M.,van Nuland, N.A. The nisin-lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics. Nat. Struct. Mol. Biol., 11:963-967, 2004 Cited by PubMed Abstract: 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. PubMed: 15361862DOI: 10.1038/nsmb830 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
