3q7t: Difference between revisions

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<StructureSection load='3q7t' size='340' side='right'caption='[[3q7t]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
<StructureSection load='3q7t' size='340' side='right'caption='[[3q7t]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3q7t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlt2 Chlt2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q7T FirstGlance]. <br>
<table><tr><td colspan='2'>[[3q7t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydia_trachomatis_434/Bu Chlamydia trachomatis 434/Bu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q7T FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3q7r|3q7r]], [[3q7s|3q7s]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTLon_0888 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=471472 CHLT2])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3q7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q7t OCA], [https://pdbe.org/3q7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q7t RCSB], [https://www.ebi.ac.uk/pdbsum/3q7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q7t ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3q7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q7t OCA], [https://pdbe.org/3q7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q7t RCSB], [https://www.ebi.ac.uk/pdbsum/3q7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q7t ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/CHXR_CHLT2 CHXR_CHLT2] May be a global positive regulator of transcription (PubMed:21057008). Binds a cis-acting element of its own promoter DNA sequence and is hence probably also involved in its own transcription activation (PubMed:21057008, PubMed:21775428, PubMed:24646934). The recognition sequence is 5'-WHGAWNH-N(3-5)-WHGAWNH-3', where W is A/T, H is C/A/T, N is G/C/A/T and the linker length in the middle is 3 to 5 nucleotides (PubMed:21057008).<ref>PMID:21057008</ref> <ref>PMID:21775428</ref> <ref>PMID:24646934</ref>  
Typically as a result of phosphorylation, OmpR/PhoB response regulators form homodimers through a receiver domain as an integral step in transcriptional activation. Phosphorylation stabilizes the ionic and hydrophobic interactions between monomers. Recent studies have shown that some response regulators retain functional activity in the absence of phosphorylation and are termed atypical response regulators. The two currently available receiver domain structures of atypical response regulators are very similar to their phospho-accepting homologs, and their propensity to form homodimers is generally retained. An atypical response regulator, ChxR, from Chlamydia trachomatis, was previously reported to form homodimers; however, the residues critical to this interaction have not been elucidated. We hypothesize that the intra- and intermolecular interactions involved in forming a transcriptionally competent ChxR are distinct from the canonical phosphorylation (activation) paradigm in the OmpR/PhoB response regulator subfamily. To test this hypothesis, structural and functional studies were performed on the receiver domain of ChxR. Two crystal structures of the receiver domain were solved with the recently developed method using triiodo compound I3C. These structures revealed many characteristics unique to OmpR/PhoB subfamily members: typical or atypical. Included was the absence of two alpha-helices present in all other OmpR/PhoB response regulators. Functional studies on various dimer interface residues demonstrated that ChxR forms relatively stable homodimers through hydrophobic interactions, and disruption of these can be accomplished with the introduction of a charged residue within the dimer interface. A gel shift study with monomeric ChxR supports that dimerization through the receiver domain is critical for interaction with DNA.
 
The atypical response regulator protein ChxR has structural characteristics and dimer interface interactions that are unique within the OmpR/PhoB subfamily.,Hickey JM, Lovell S, Battaile KP, Hu L, Middaugh CR, Hefty PS J Biol Chem. 2011 Sep 16;286(37):32606-16. Epub 2011 Jul 20. PMID:21775428<ref>PMID:21775428</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3q7t" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Chlt2]]
[[Category: Chlamydia trachomatis 434/Bu]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Battaile, K P]]
[[Category: Battaile KP]]
[[Category: Hefty, P S]]
[[Category: Hefty PS]]
[[Category: Hickey, J]]
[[Category: Hickey J]]
[[Category: Hu, L]]
[[Category: Hu L]]
[[Category: Lovell, S]]
[[Category: Lovell S]]
[[Category: Middaugh, C R]]
[[Category: Middaugh CR]]
[[Category: Chlamydia]]
[[Category: Chxr]]
[[Category: Ompr]]
[[Category: Receiver domain]]
[[Category: Transcription]]
[[Category: Transcription factor]]

Latest revision as of 13:46, 21 February 2024

2.15A resolution structure (I41 Form) of the ChxR receiver domain from Chlamydia trachomatis2.15A resolution structure (I41 Form) of the ChxR receiver domain from Chlamydia trachomatis

Structural highlights

3q7t is a 2 chain structure with sequence from Chlamydia trachomatis 434/Bu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.15Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CHXR_CHLT2 May be a global positive regulator of transcription (PubMed:21057008). Binds a cis-acting element of its own promoter DNA sequence and is hence probably also involved in its own transcription activation (PubMed:21057008, PubMed:21775428, PubMed:24646934). The recognition sequence is 5'-WHGAWNH-N(3-5)-WHGAWNH-3', where W is A/T, H is C/A/T, N is G/C/A/T and the linker length in the middle is 3 to 5 nucleotides (PubMed:21057008).[1] [2] [3]

References

  1. ↑ Hickey JM, Weldon L, Hefty PS. The atypical OmpR/PhoB response regulator ChxR from Chlamydia trachomatis forms homodimers in vivo and binds a direct repeat of nucleotide sequences. J Bacteriol. 2011 Jan;193(2):389-98. PMID:21057008 doi:10.1128/JB.00833-10
  2. ↑ Hickey JM, Lovell S, Battaile KP, Hu L, Middaugh CR, Hefty PS. The atypical response regulator protein ChxR has structural characteristics and dimer interface interactions that are unique within the OmpR/PhoB subfamily. J Biol Chem. 2011 Sep 16;286(37):32606-16. Epub 2011 Jul 20. PMID:21775428 doi:10.1074/jbc.M111.220574
  3. ↑ Barta ML, Hickey JM, Anbanandam A, Dyer K, Hammel M, Hefty PS. Atypical response regulator ChxR from Chlamydia trachomatis is structurally poised for DNA binding. PLoS One. 2014 Mar 19;9(3):e91760. doi: 10.1371/journal.pone.0091760. eCollection, 2014. PMID:24646934 doi:http://dx.doi.org/10.1371/journal.pone.0091760

3q7t, resolution 2.15Å

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