{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,19]],"date-time":"2026-08-19T17:40:25Z","timestamp":1787161225767,"version":"build-2736575974"},"reference-count":41,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2014,11,20]],"date-time":"2014-11-20T00:00:00Z","timestamp":1416441600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100001332","name":"CSIR","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100001332","id-type":"DOI","asserted-by":"crossref"}]},{"name":"DBT, Government of India"}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2015,1]]},"abstract":"\n \n \n The growing emergence of antibiotic\u2010resistant bacteria has led to the exploration of naturally occurring defense peptides as antimicrobials. In this study, we found that laterosporulin (\n LS<\/jats:styled-content>\n ), a class\n II<\/jats:styled-content>\n d bacteriocin, effectively kills active and nonmultiplying cells of both Gram\u2010positive and Gram\u2010negative bacteria. Fluorescence and electron microscopy suggest that growth inhibition occurs because of increased membrane permeability. The crystal structure of\n LS<\/jats:styled-content>\n at 2.0\u00a0\u00c5 resolution reveals an all\u2010\u03b2 conformation of this peptide, with four \u03b2\u2010strands forming a twisted \u03b2\u2010sheet. All six intrinsic cysteines are intramolecularly disulfide\u2010bonded, with two disulfides constraining the N terminus of the peptide and the third disulfide crosslinking the extreme C terminus, resulting in the formation of a closed structure. The significance of disulfides in maintaining the in\u2010solution peptide structure was confirmed by\n CD<\/jats:styled-content>\n and fluorescence analyses. Despite a low overall sequence similarity,\n LS<\/jats:styled-content>\n has disulfide connectivity [\n \n C\n I<\/jats:sup>\n <\/jats:styled-content>\n \u2013\n \n C\n V<\/jats:sup>\n <\/jats:styled-content>\n ,\n \n C\n II<\/jats:sup>\n <\/jats:styled-content>\n \u2013\n \n C\n IV<\/jats:sup>\n <\/jats:styled-content>\n , and\n \n C\n III<\/jats:sup>\n <\/jats:styled-content>\n \u2013\n \n C\n VI<\/jats:sup>\n <\/jats:styled-content>\n ] like that of \u03b2\u2010defensins and a striking architectural similarity with \u03b1\u2010defensins. Therefore\n LS<\/jats:styled-content>\n presents a missing link between bacteriocins and mammalian defensins, and is also a potential antimicrobial lead, in particular against nonmultiplying bacteria.\n <\/jats:p>\n <\/jats:sec>\n \n Database<\/jats:title>\n \n The atomic coordinates and the structure factors have been deposited in the Protein Data Bank under accession number\n 4OZK<\/jats:ext-link>\n <\/jats:p>\n <\/jats:sec>","DOI":"10.1111\/febs.13129","type":"journal-article","created":{"date-parts":[[2014,10,27]],"date-time":"2014-10-27T07:38:30Z","timestamp":1414395510000},"page":"203-214","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":38,"title":["The intramolecular disulfide\u2010stapled structure of laterosporulin, a class\n II<\/scp>\n d bacteriocin, conceals a human defensin\u2010like structural module"],"prefix":"10.1111","volume":"282","author":[{"given":"Pradip Kumar","family":"Singh","sequence":"first","affiliation":[{"name":"Microbial Type Culture Collection & Gene Bank CSIR\u2010Institute of Microbial Technology Chandigarh India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vipul","family":"Solanki","sequence":"additional","affiliation":[{"name":"G.N. 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