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Signaling through the Lqs system occurs through the \u03b1\u2010hydroxyketone compound <jats:italic>Legionella<\/jats:italic> autoinducer\u20101 (LAI\u20101) and converges on the prototypic response regulator LqsR, which dimerizes upon phosphorylation of the conserved aspartate, D<jats:sub>108<\/jats:sub>. In this study, we determine the high\u2010resolution structure of monomeric LqsR. The structure reveals a receiver domain adopting a canonical (\u03b2\u03b1)<jats:sub>5<\/jats:sub> fold, which is connected through an additional sixth helix and an extended \u03b15\u2010helix to a novel output domain. The two domains delineate a mainly positively charged groove, and the output domain adopts a five\u2010stranded antiparallel \u03b2\u2010sheet fold similar to nucleotide\u2010binding proteins. Structure\u2010based mutagenesis identified amino acids critical for LqsR phosphorylation and dimerization. Upon phosphorylation, the LqsR<jats:sub>D172A<\/jats:sub> and LqsR<jats:sub>D302N\/E303Q<\/jats:sub> mutant proteins dimerized even more readily than wild\u2010type LqsR, and no evidence for semi\u2010phosphorylated heterodimers was obtained. Taken together, the high\u2010resolution structure of LqsR reveals functionally relevant amino acid residues implicated in signal transduction of the prototypic response regulator.<\/jats:p>","DOI":"10.1111\/mmi.14477","type":"journal-article","created":{"date-parts":[[2020,1,30]],"date-time":"2020-01-30T02:26:45Z","timestamp":1580351205000},"page":"1070-1084","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":17,"title":["The structure of the <i>Legionella<\/i> response regulator LqsR reveals amino acids critical for phosphorylation and dimerization"],"prefix":"10.1111","volume":"113","author":[{"given":"Ramon","family":"Hochstrasser","sequence":"first","affiliation":[{"name":"Institute of Medical Microbiology University of Z\u00fcrich Z\u00fcrich Switzerland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cedric A. 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