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<StructureSection load='1h0m' size='340' side='right'caption='[[1h0m]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='1h0m' size='340' side='right'caption='[[1h0m]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1h0m]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"achromobacter_radiobacter"_(beijerinck_and_van_delden_1902)_bergey_et_al._1934 "achromobacter radiobacter" (beijerinck and van delden 1902) bergey et al. 1934]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H0M OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1H0M FirstGlance]. <br>
<table><tr><td colspan='2'>[[1h0m]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H0M FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LAE:3-OXO-OCTANOIC+ACID+(2-OXO-TETRAHYDRO-FURAN-3-YL)-AMIDE'>LAE</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]] 3&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LAE:3-OXO-OCTANOIC+ACID+(2-OXO-TETRAHYDRO-FURAN-3-YL)-AMIDE'>LAE</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1l3l|1l3l]]</div></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=1h0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h0m OCA], [https://pdbe.org/1h0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h0m RCSB], [https://www.ebi.ac.uk/pdbsum/1h0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h0m ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">traR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=358 "Achromobacter radiobacter" (Beijerinck and van Delden 1902) Bergey et al. 1934])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1h0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h0m OCA], [http://pdbe.org/1h0m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h0m RCSB], [http://www.ebi.ac.uk/pdbsum/1h0m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h0m ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TRAR_RHIRD TRAR_RHIRD]] Positive regulation of conjugal transfer of Ti plasmids. TraR activates target genes in the presence of AAI and also activates traR and traI themselves.  
[https://www.uniprot.org/uniprot/TRAR_RHIRD TRAR_RHIRD] Positive regulation of conjugal transfer of Ti plasmids. TraR activates target genes in the presence of AAI and also activates traR and traI themselves.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1h0m ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1h0m ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The quorum sensing system allows bacteria to sense their cell density and initiate an altered pattern of gene expression after a sufficient quorum of cells has accumulated. In Agrobacterium tumefaciens, quorum sensing controls conjugal transfer of the tumour- inducing plasmid, responsible for plant crown gall disease. The core components of this system are the transcriptional regulator TraR and its inducing ligand N-(3-oxo-octanoyl)-L-homoserine lactone. This complex binds DNA and activates gene expression. We have determined the crystal structure of TraR in complex with its autoinducer and target DNA (PDB code 1h0m). The protein is dimeric, with each monomer composed of an N-terminal domain, which binds the ligand in an enclosed cavity far from the dimerization region, and a C-terminal domain, which binds DNA via a helix-turn-helix motif. The structure reveals an asymmetric homodimer, with one monomer longer than the other. The N-terminal domain resembles GAF/PAS domains, normally fused to catalytic signalling domains. In TraR, the gene fusion is between a GAF/PAS domain and a DNA-binding domain, resulting in a specific transcriptional regulator involved in quorum sensing.
The crystal structure of the quorum sensing protein TraR bound to its autoinducer and target DNA.,Vannini A, Volpari C, Gargioli C, Muraglia E, Cortese R, De Francesco R, Neddermann P, Marco SD EMBO J. 2002 Sep 2;21(17):4393-401. PMID:12198141<ref>PMID:12198141</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1h0m" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Agrobacterium tumefaciens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cortese, R]]
[[Category: Synthetic construct]]
[[Category: Francesco, R De]]
[[Category: Cortese R]]
[[Category: Gargioli, C]]
[[Category: De Francesco R]]
[[Category: Marco, S Di]]
[[Category: Di Marco S]]
[[Category: Muraglia, E]]
[[Category: Gargioli C]]
[[Category: Neddermann, P]]
[[Category: Muraglia E]]
[[Category: Vannini, A]]
[[Category: Neddermann P]]
[[Category: Volpari, C]]
[[Category: Vannini A]]
[[Category: Dna-binding protein]]
[[Category: Volpari C]]
[[Category: Homoserine lactone]]
[[Category: Luxr-type protein]]
[[Category: Quorum sensing]]
[[Category: Transcription-dna complex]]
[[Category: Transcription/dna]]
[[Category: Transcriptional regulator]]
[[Category: Trar]]

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