{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,15]],"date-time":"2026-01-15T05:28:54Z","timestamp":1768454934122,"version":"3.49.0"},"reference-count":41,"publisher":"Proceedings of the National Academy of Sciences","issue":"21","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2000,10,10]]},"abstract":"<jats:p>\n            The solution structure of bacteriocin AS-48, a 70-residue cyclic\n polypeptide from\n            <jats:italic>Enterococcus faecalis<\/jats:italic>\n            , consists of a\n globular arrangement of five \u03b1-helices enclosing a compact\n hydrophobic core. The head-to-tail union lies in the middle of helix 5,\n a fact that is shown to have a pronounced effect on the stability of\n the three-dimensional structure. Positive charges in the side chains of\n residues in helix 4 and in the turn linking helix 4 to helix 5 form a\n cluster that most probably determine its antibacterial activity by\n promoting pore formation in cell membranes. A similar five-helix\n structural motif has been found in the antimicrobial NK-lysin, an\n effector polypeptide of T and natural killer (NK) cells. Bacteriocin\n AS-48 lacks the three disulfide bridges characteristic of the saposin\n fold present in NK-lysin, and has no sequence homology with it.\n Nevertheless, the similar molecular architecture and high positive\n charge strongly suggest a common mechanism of antibacterial action.\n          <\/jats:p>","DOI":"10.1073\/pnas.210301097","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T14:32:33Z","timestamp":1027693953000},"page":"11221-11226","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":149,"title":["Bacteriocin AS-48, a microbial cyclic polypeptide structurally and functionally related to mammalian NK-lysin"],"prefix":"10.1073","volume":"97","author":[{"given":"Carlos","family":"Gonz\u00e1lez","sequence":"first","affiliation":[{"name":"Instituto de Estructura de la Materia, Consejo Superior de\r Investigaciones Cient\u00edficas, Madrid 28006, Spain;\r Area de Microbiolog\u00eda, Facultad de Ciencias\r Experimentales, Universidad de Ja\u00e9n, Ja\u00e9n 23071, Spain; and\r Departamento de Microbiolog\u00eda, Facultad de\r Ciencias, Universidad de Granada, Granada 18071, Spain"}]},{"given":"Grant M.","family":"Langdon","sequence":"additional","affiliation":[{"name":"Instituto de Estructura de la Materia, Consejo Superior de\r Investigaciones Cient\u00edficas, Madrid 28006, Spain;\r Area de Microbiolog\u00eda, Facultad de Ciencias\r Experimentales, Universidad de Ja\u00e9n, Ja\u00e9n 23071, Spain; and\r Departamento de Microbiolog\u00eda, Facultad de\r Ciencias, Universidad de Granada, Granada 18071, Spain"}]},{"given":"Marta","family":"Bruix","sequence":"additional","affiliation":[{"name":"Instituto de Estructura de la Materia, Consejo Superior de\r Investigaciones Cient\u00edficas, Madrid 28006, Spain;\r Area de Microbiolog\u00eda, Facultad de Ciencias\r Experimentales, Universidad de Ja\u00e9n, Ja\u00e9n 23071, Spain; and\r Departamento de Microbiolog\u00eda, Facultad de\r Ciencias, Universidad de Granada, Granada 18071, Spain"}]},{"given":"Antonio","family":"G\u00e1lvez","sequence":"additional","affiliation":[{"name":"Instituto de Estructura de la Materia, Consejo Superior de\r Investigaciones Cient\u00edficas, Madrid 28006, Spain;\r Area de Microbiolog\u00eda, Facultad de Ciencias\r Experimentales, Universidad de Ja\u00e9n, Ja\u00e9n 23071, Spain; 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