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PLoS One. 2014 Mar 19;9(3):e91760. doi: 10.1371/journal.pone.0091760. eCollection 2014.

Atypical response regulator ChxR from Chlamydia trachomatis is structurally poised for DNA binding.

Author information

1
Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas, United States of America.
2
Department of Pharmaceutical Chemistry, University of Kansas, Lawrence, Kansas, United States of America.
3
Del Shankel Structural Biology Center, University of Kansas, Lawrence, Kansas, United States of America.
4
Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California, United States of America.

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.

PMID:
24646934
PMCID:
PMC3960148
DOI:
10.1371/journal.pone.0091760
[Indexed for MEDLINE]
Free PMC Article

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