{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T17:03:09Z","timestamp":1791046989745,"version":"4.1.0"},"reference-count":60,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2012,1,10]],"date-time":"2012-01-10T00:00:00Z","timestamp":1326153600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2012,2]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>Expression of the two critical virulence factors of <jats:italic>Vibrio cholerae<\/jats:italic>, toxin\u2010coregulated pilus and cholera toxin, is initiated at the <jats:italic>tcpPH<\/jats:italic> promoter by the regulators AphA and AphB. AphA is a winged helix DNA\u2010binding protein that enhances the ability of AphB, a LysR\u2010type transcriptional regulator, to activate <jats:italic>tcpPH<\/jats:italic> expression. We present here the 2.2\u2003\u00c5 X\u2010ray crystal structure of full\u2010length AphB. As reported for other LysR\u2010type proteins, AphB is a tetramer with two distinct subunit conformations. Unlike other family members, AphB must undergo a significant conformational change in order to bind to DNA. We have found five independent mutations in the putative ligand\u2010binding pocket region that allow AphB to constitutively activate <jats:italic>tcpPH<\/jats:italic> expression at the non\u2010permissive pH of 8.5 and in the presence of oxygen. These findings indicate that AphB is responsive to intracellular pH as well as to anaerobiosis and that residues in the ligand\u2010binding pocket of the protein influence its ability to respond to both of these signals. We have solved the structure of one of the constitutive mutants, and observe conformational changes that would allow DNA binding. Taken together, these results describe a pathway of conformational changes allowing communication between the ligand and DNA binding regions of AphB.<\/jats:p>","DOI":"10.1111\/j.1365-2958.2011.07919.x","type":"journal-article","created":{"date-parts":[[2011,11,7]],"date-time":"2011-11-07T06:56:59Z","timestamp":1320649019000},"page":"457-470","source":"Crossref","is-referenced-by-count":59,"title":["The crystal structure of AphB, a virulence gene activator from <i>Vibrio cholerae<\/i>, reveals residues that influence its response to oxygen and pH"],"prefix":"10.1111","volume":"83","author":[{"given":"Jennifer L.","family":"Taylor","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rukman S.","family":"De Silva","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gabriela","family":"Kovacikova","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wei","family":"Lin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ronald K.","family":"Taylor","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karen","family":"Skorupski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"F. 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