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http://purl.uniprot.org/citations/26712005http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26712005http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26712005http://www.w3.org/2000/01/rdf-schema#comment"Bacterial biofilm formation during chronic infections confers increased fitness, antibiotic tolerance, and cytotoxicity. In many pathogens, the transition from a planktonic lifestyle to collaborative, sessile biofilms represents a regulated process orchestrated by the intracellular second-messenger c-di-GMP. A main effector for c-di-GMP signaling in the opportunistic pathogen Pseudomonas aeruginosa is the transcription regulator FleQ. FleQ is a bacterial enhancer-binding protein (bEBP) with a central AAA+ ATPase σ(54)-interaction domain, flanked by a C-terminal helix-turn-helix DNA-binding motif and a divergent N-terminal receiver domain. Together with a second ATPase, FleN, FleQ regulates the expression of flagellar and exopolysaccharide biosynthesis genes in response to cellular c-di-GMP. Here we report structural and functional data that reveal an unexpected mode of c-di-GMP recognition that is associated with major conformational rearrangements in FleQ. Crystal structures of FleQ's AAA+ ATPase domain in its apo-state or bound to ADP or ATP-γ-S show conformations reminiscent of the activated ring-shaped assemblies of other bEBPs. As revealed by the structure of c-di-GMP-complexed FleQ, the second messenger interacts with the AAA+ ATPase domain at a site distinct from the ATP binding pocket. c-di-GMP interaction leads to active site obstruction, hexameric ring destabilization, and discrete quaternary structure transitions. Solution and cell-based studies confirm coupling of the ATPase active site and c-di-GMP binding, as well as the functional significance of crystallographic interprotomer interfaces. Taken together, our data offer unprecedented insight into conserved regulatory mechanisms of gene expression under direct c-di-GMP control via FleQ and FleQ-like bEBPs."xsd:string
http://purl.uniprot.org/citations/26712005http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1523148113"xsd:string
http://purl.uniprot.org/citations/26712005http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1523148113"xsd:string
http://purl.uniprot.org/citations/26712005http://purl.uniprot.org/core/author"Harwood C.S."xsd:string
http://purl.uniprot.org/citations/26712005http://purl.uniprot.org/core/author"Harwood C.S."xsd:string
http://purl.uniprot.org/citations/26712005http://purl.uniprot.org/core/author"Navarro M.V."xsd:string
http://purl.uniprot.org/citations/26712005http://purl.uniprot.org/core/author"Navarro M.V."xsd:string
http://purl.uniprot.org/citations/26712005http://purl.uniprot.org/core/author"Sondermann H."xsd:string
http://purl.uniprot.org/citations/26712005http://purl.uniprot.org/core/author"Sondermann H."xsd:string
http://purl.uniprot.org/citations/26712005http://purl.uniprot.org/core/author"Baraquet C."xsd:string
http://purl.uniprot.org/citations/26712005http://purl.uniprot.org/core/author"Baraquet C."xsd:string
http://purl.uniprot.org/citations/26712005http://purl.uniprot.org/core/author"Krasteva P.V."xsd:string
http://purl.uniprot.org/citations/26712005http://purl.uniprot.org/core/author"Krasteva P.V."xsd:string
http://purl.uniprot.org/citations/26712005http://purl.uniprot.org/core/author"Matsuyama B.Y."xsd:string
http://purl.uniprot.org/citations/26712005http://purl.uniprot.org/core/author"Matsuyama B.Y."xsd:string
http://purl.uniprot.org/citations/26712005http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/26712005http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/26712005http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/26712005http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/26712005http://purl.uniprot.org/core/pages"E209-E218"xsd:string
http://purl.uniprot.org/citations/26712005http://purl.uniprot.org/core/pages"E209-E218"xsd:string
http://purl.uniprot.org/citations/26712005http://purl.uniprot.org/core/title"Mechanistic insights into c-di-GMP-dependent control of the biofilm regulator FleQ from Pseudomonas aeruginosa."xsd:string
http://purl.uniprot.org/citations/26712005http://purl.uniprot.org/core/title"Mechanistic insights into c-di-GMP-dependent control of the biofilm regulator FleQ from Pseudomonas aeruginosa."xsd:string
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