Atypical Response Regulator ChxR from Chlamydia trachomatis Is Structurally Poised for DNA Binding
dc.contributor.author | Barta, Michael L. | |
dc.contributor.author | Hickey, John M. | |
dc.contributor.author | Anbanandam, Asokan | |
dc.contributor.author | Dyer, Kevin | |
dc.contributor.author | Hammel, Michal | |
dc.contributor.author | Hefty, P. Scott | |
dc.date.accessioned | 2014-04-28T17:42:02Z | |
dc.date.available | 2014-04-28T17:42:02Z | |
dc.date.issued | 2014-03-19 | |
dc.identifier.citation | Barta ML, Hickey JM, Anbanandam A, Dyer K, Hammel M, et al. (2014) Atypical Response Regulator ChxR from Chlamydia trachomatis Is Structurally Poised for DNA Binding. PLoS ONE 9(3): e91760. http://dx.doi.org/10.1371/journal.pone.0091760 | |
dc.identifier.uri | http://hdl.handle.net/1808/13605 | |
dc.description.abstract | ChxR 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. | |
dc.description.sponsorship | NIH AIR01079083. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. | |
dc.publisher | Public Library of Science | |
dc.rights | ©2014 Barta et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. | |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | |
dc.subject | DNA sequences | |
dc.subject | DNA structure | |
dc.subject | DNA-binding proteins | |
dc.subject | Nuclear magnetic resonance | |
dc.subject | Phosphorylation | |
dc.subject | Protein structure | |
dc.subject | Sequence alignment | |
dc.subject | Small-angle scattering | |
dc.title | Atypical Response Regulator ChxR from Chlamydia trachomatis Is Structurally Poised for DNA Binding | |
dc.type | Article | |
kusw.kuauthor | Barta, Michael L. | |
kusw.kuauthor | Hickey, John M. | |
kusw.kuauthor | Anbanandam, Asokan | |
kusw.kuauthor | Hefty, P. Scott | |
kusw.kudepartment | Molecular Biosciences | |
kusw.kudepartment | Pharmaceutical Chemistry | |
kusw.kudepartment | Del Shankel Structural Biology Center | |
kusw.oastatus | fullparticipation | |
dc.identifier.doi | 10.1371/journal.pone.0091760 | |
kusw.oaversion | Scholarly/refereed, publisher version | |
kusw.oapolicy | This item meets KU Open Access policy criteria. | |
dc.rights.accessrights | openAccess |
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Except where otherwise noted, this item's license is described as: ©2014 Barta et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.