{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,8,8]],"date-time":"2024-08-08T10:38:29Z","timestamp":1723113509260},"reference-count":20,"publisher":"American Society for Microbiology","issue":"18","license":[{"start":{"date-parts":[[2011,9,15]],"date-time":"2011-09-15T00:00:00Z","timestamp":1316044800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2011,9,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The intermolecular interactions of the mycobacteriophage Ms6 secretion chaperone with endolysin were characterized. The 384-amino-acid lysin (lysin\n            <jats:sub>384<\/jats:sub>\n            )-binding domain was found to encompass the N-terminal region of Gp1, which is also essential for a lysis phenotype in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Escherichia coli<\/jats:named-content>\n            . In addition, a GXXXG-like motif involved in Gp1 homo-oligomerization was identified within the C-terminal region.\n          <\/jats:p>","DOI":"10.1128\/jb.00380-11","type":"journal-article","created":{"date-parts":[[2011,7,16]],"date-time":"2011-07-16T07:11:02Z","timestamp":1310800262000},"page":"5002-5006","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":13,"title":["The Endolysin-Binding Domain Encompasses the N-Terminal Region of the Mycobacteriophage Ms6 Gp1 Chaperone"],"prefix":"10.1128","volume":"193","author":[{"given":"Maria Jo\u00e3o","family":"Catal\u00e3o","sequence":"first","affiliation":[{"name":"Centro de Patog\u00e9nese Molecular, Unidade dos Retrov\u00edrus e Infec\u00e7\u00f5es Associadas, Faculty of Pharmacy, University of Lisbon, Av. 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