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Título: | Bacteriocin AS-48, a microbial cyclic polypeptide structurally and functionally related to mammalian NK-lysin |
Autor: | González, Carlos CSIC ; Langdon, Grant M.; Bruix, M. CSIC ORCID ; Gálvez, Antonio; Valdivia, E.; Maqueda, Mercedes; Rico, Manuel CSIC | Palabras clave: | Cationic antibacterial peptides NMR solution structure Five-helix globule Cyclic Polypeptide Membrane permeation |
Fecha de publicación: | 10-oct-2000 | Editor: | National Academy of Sciences (U.S.) | Citación: | Proceedings of the National Academy of Sciences of the United States of America 97(10): 11221-11226 (2000) | Resumen: | The solution structure of bacteriocin AS-48, a 70-residue cyclic polypeptide from Enterococcus faecalis, consists of a globular arrangement of five α-helices enclosing a compact hydrophobic core. The head-to-tail union lies in the middle of helix 5, a fact that is shown to have a pronounced effect on the stability of the three-dimensional structure. Positive charges in the side chains of residues in helix 4 and in the turn linking helix 4 to helix 5 form a cluster that most probably determine its antibacterial activity by promoting pore formation in cell membranes. A similar five-helix structural motif has been found in the antimicrobial NK-lysin, an effector polypeptide of T and natural killer (NK) cells. Bacteriocin AS-48 lacks the three disulfide bridges characteristic of the saposin fold present in NK-lysin, and has no sequence homology with it. Nevertheless, the similar molecular architecture and high positive charge strongly suggest a common mechanism of antibacterial action. | Versión del editor: | https://doi.org/10.1073/pnas.210301097 | URI: | http://hdl.handle.net/10261/256975 | DOI: | 10.1073/pnas.210301097 | Identificadores: | doi: 10.1073/pnas.210301097 issn: 0027-8424 e-issn: 1091-6490 |
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