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dc.contributor.authorBarta, Michael L.
dc.contributor.authorHickey, John M.
dc.contributor.authorAnbanandam, Asokan
dc.contributor.authorDyer, Kevin
dc.contributor.authorHammel, Michal
dc.contributor.authorHefty, P. Scott
dc.date.accessioned2015-12-16T19:27:14Z
dc.date.available2015-12-16T19:27:14Z
dc.date.issued2014-03-19
dc.identifier.citationBarta, Michael L., John M. Hickey, Asokan Anbanandam, Kevin Dyer, Michal Hammel, and P. Scott Hefty. "Atypical Response Regulator ChxR from Chlamydia Trachomatis Is Structurally Poised for DNA Binding." PLoS ONE 9.3 (2014): n. pag. DOI:10.1371/journal.pone.0091760en_US
dc.identifier.urihttp://hdl.handle.net/1808/19240
dc.descriptionThis is the published version. Copyright Public Library of Scienceen_US
dc.description.abstractChxR is an atypical two-component signal transduction response regulator (RR) of the OmpR/PhoB subfamily encoded by the obligate intracellular bacterial pathogen Chlamydia trachomatis. Despite structural homology within both receiver and effector domains to prototypical subfamily members, ChxR does not require phosphorylation for dimer formation, DNA binding or transcriptional activation. Thus, we hypothesized that ChxR is in a conformation optimal for DNA binding with limited interdomain interactions. To address this hypothesis, the NMR solution structure of the ChxR effector domain was determined and used in combination with the previously reported ChxR receiver domain structure to generate a full-length dimer model based upon SAXS analysis. Small-angle scattering of ChxR supported a dimer with minimal interdomain interactions and effector domains in a conformation that appears to require only subtle reorientation for optimal major/minor groove DNA interactions. SAXS modeling also supported that the effector domains were in a head-to-tail conformation, consistent with ChxR recognizing tandem DNA repeats. The effector domain structure was leveraged to identify key residues that were critical for maintaining protein - nucleic acid interactions. In combination with prior analysis of the essential location of specific nucleotides for ChxR recognition of DNA, a model of the full-length ChxR dimer bound to its cognate cis-acting element was generated.en_US
dc.publisherPublic Library of Scienceen_US
dc.subjectSmall-angle scatteringen_US
dc.subjectProtein structureen_US
dc.subjectPhosphorylationen_US
dc.subjectSequence alignmenten_US
dc.subjectDNA structureen_US
dc.subjectSequence motif analysisen_US
dc.subjectDNA-binding proteinsen_US
dc.subjectRoot structureen_US
dc.titleAtypical Response Regulator ChxR from Chlamydia trachomatis Is Structurally Poised for DNA Bindingen_US
dc.typeArticle
kusw.kuauthorAnbanandam, Asokan
kusw.kudepartmentHiguchi Biosciences Centeren_US
dc.identifier.doi10.1371/journal.pone.0091760
kusw.oaversionScholarly/refereed, publisher version
kusw.oapolicyThis item meets KU Open Access policy criteria.
dc.rights.accessrightsopenAccess


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