{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,19]],"date-time":"2026-02-19T06:23:03Z","timestamp":1771482183203,"version":"3.50.1"},"reference-count":49,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2009,6,17]],"date-time":"2009-06-17T00:00:00Z","timestamp":1245196800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Proteins"],"published-print":{"date-parts":[[2009,11]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The type IVb pilus of the enteropathogenic bacteria <jats:italic>Salmonella typhi<\/jats:italic> is a major adhesion factor during the entry of this pathogen into gastrointestinal epithelial cells. Its target of adhesion is a stretch of 10 residues from the first extracellular domain of cystic fibrosis transmembrane conductance regulator (CFTR). The crystal structure of the N\u2010terminal 25 amino acid deleted <jats:italic>S. typhi<\/jats:italic> native PilS protein (\u0394PilS), which makes the pilus, was determined at 1.9 \u00c5 resolution by the multiwavelength anomalous dispersion method. Also, the structure of the complex of \u0394PilS and a target CFTR peptide, determined at 1.8 \u00c5, confirms that residues 113\u2013117 (NKEER) of CFTR are involved in binding with the pilin protein and gives us insight on the amino acids that are essential for binding. Furthermore, we have also explored the role of a conserved disulfide bridge in pilus formation. The subunit structure and assembly architecture are crucial for understanding pilus functions and designing suitable therapeutics against typhoid. Proteins 2009. \u00a9 2009 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/prot.22500","type":"journal-article","created":{"date-parts":[[2009,6,17]],"date-time":"2009-06-17T22:22:55Z","timestamp":1245277375000},"page":"253-261","source":"Crossref","is-referenced-by-count":11,"title":["Structural basis of typhoid: <i>Salmonella typhi<\/i> type IVb pilin (PilS) and cystic fibrosis transmembrane conductance regulator interaction"],"prefix":"10.1002","volume":"77","author":[{"given":"Asha M.","family":"Balakrishna","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anand M.","family":"Saxena","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Henry Yu\u2010Keung","family":"Mok","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kunchithapadam","family":"Swaminathan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2009,7,22]]},"reference":[{"key":"e_1_2_6_2_2","doi-asserted-by":"crossref","first-page":"15703","DOI":"10.1016\/S0021-9258(18)66774-2","article-title":"Nucleotide sequence transcriptional initiation site of two Pseudomonas aeruginosa pilin genes","volume":"261","author":"Johnson K","year":"1986","journal-title":"J Biol Chem"},{"key":"e_1_2_6_3_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.81.19.6110"},{"key":"e_1_2_6_4_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.1988.tb00073.x"},{"key":"e_1_2_6_5_2","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1128\/jb.163.1.132-139.1985","article-title":"Cloning sequencing of a Moraxella bovis pilin gene","volume":"163","author":"Marrs CF","year":"1985","journal-title":"J Bacteriol"},{"key":"e_1_2_6_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.172.8.4370-4377.1990"},{"key":"e_1_2_6_7_2","doi-asserted-by":"publisher","DOI":"10.1099\/00221287-137-10-2483"},{"key":"e_1_2_6_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/0002-9343(90)90260-K"},{"key":"e_1_2_6_9_2","first-page":"1909","article-title":"Sequence divergence in two tandemly located pilin genes of Eikenella corrodens. 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