2m1b: Difference between revisions
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==Solution structure of the CHXR DNA-binding domain== | |||
=== | <StructureSection load='2m1b' size='340' side='right' caption='[[2m1b]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2m1b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chltc Chltc]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M1B OCA]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTL0894, CTL2C_660 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=887712 CHLTC])</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2m1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m1b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2m1b RCSB], [http://www.ebi.ac.uk/pdbsum/2m1b PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
Atypical response regulator ChxR from Chlamydia trachomatis is structurally poised for DNA binding.,Barta ML, Hickey JM, Anbanandam A, Dyer K, Hammel M, Hefty PS PLoS One. 2014 Mar 19;9(3):e91760. doi: 10.1371/journal.pone.0091760. eCollection, 2014. PMID:24646934<ref>PMID:24646934</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Chltc]] | |||
[[Category: Anbanandam, A M.]] | [[Category: Anbanandam, A M.]] | ||
[[Category: Hefty, S P.]] | [[Category: Hefty, S P.]] | ||
Revision as of 09:57, 14 May 2014
Solution structure of the CHXR DNA-binding domainSolution structure of the CHXR DNA-binding domain
Structural highlights
Publication Abstract from PubMedChxR 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. Atypical response regulator ChxR from Chlamydia trachomatis is structurally poised for DNA binding.,Barta ML, Hickey JM, Anbanandam A, Dyer K, Hammel M, Hefty PS PLoS One. 2014 Mar 19;9(3):e91760. doi: 10.1371/journal.pone.0091760. eCollection, 2014. PMID:24646934[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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