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2y7p

From Proteopedia

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<StructureSection load='2y7p' size='340' side='right'caption='[[2y7p]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='2y7p' size='340' side='right'caption='[[2y7p]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2y7p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_sp._dnt Burkholderia sp. dnt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y7P OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2Y7P FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2y7p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_sp._DNT Burkholderia sp. DNT]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y7P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y7P FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEU:2,5,8,11,14,17,20,23,26,29,32,35,38,41,44,47,50,53,56,59,62,65,68,71,74,77,80-HEPTACOSAOXADOOCTACONTAN-82-OL'>PEU</scene>, <scene name='pdbligand=SAL:2-HYDROXYBENZOIC+ACID'>SAL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1uth|1uth]], [[2y7w|2y7w]], [[1utb|1utb]], [[2y7r|2y7r]], [[2y84|2y84]], [[2y7k|2y7k]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEU:2,5,8,11,14,17,20,23,26,29,32,35,38,41,44,47,50,53,56,59,62,65,68,71,74,77,80-HEPTACOSAOXADOOCTACONTAN-82-OL'>PEU</scene>, <scene name='pdbligand=SAL:2-HYDROXYBENZOIC+ACID'>SAL</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2y7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y7p OCA], [http://pdbe.org/2y7p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2y7p RCSB], [http://www.ebi.ac.uk/pdbsum/2y7p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2y7p ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2y7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y7p OCA], [https://pdbe.org/2y7p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y7p RCSB], [https://www.ebi.ac.uk/pdbsum/2y7p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y7p ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q7WT50_9BURK Q7WT50_9BURK]
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Activation of LysR-type transcription factors (LTTRs) is thought to result from conformational changes that occur when inducer molecules bind to their Inducer Binding Domains (IBDs). However, the exact nature of these changes remains to be fully elucidated. We present the crystal structures of two truncated constructs of the LTTR DntR in their apo- forms and in complex with its natural inducer molecule, salicylate. These provide a fuller picture of the conformational changes that can occur in LTTR IBDs and offer insights that may be relevant when considering the mechanism of activation of LTTRs. Two of the crystal structures show that DntR IBDs can bind up to two inducer molecules. The full extent of conformational changes observed is achieved only when inducer molecules are bound in both binding sites identified. Point mutations disrupting the putative secondary binding site produce DntR variants with a reduced response to salicylate in a whole cell system, suggesting that this site is functionally relevant.
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Crystal structures of DntR inducer binding domains in complex with salicylate offer insights into the activation of LysR-type transcriptional regulators.,Devesse L, Smirnova I, Lonneborg R, Kapp U, Brzezinski P, Leonard GA, Dian C Mol Microbiol. 2011 Jul;81(2):354-367. doi:, 10.1111/j.1365-2958.2011.07673.x. Epub 2011 Jun 22. PMID:21692874<ref>PMID:21692874</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2y7p" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Burkholderia sp. dnt]]
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[[Category: Burkholderia sp. DNT]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Brzezinski, P]]
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[[Category: Brzezinski P]]
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[[Category: Devesse, L]]
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[[Category: Devesse L]]
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[[Category: Dian, C]]
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[[Category: Dian C]]
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[[Category: Kapp, U]]
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[[Category: Kapp U]]
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[[Category: Leonard, G A]]
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[[Category: Leonard GA]]
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[[Category: Lonneborg, R]]
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[[Category: Lonneborg R]]
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[[Category: Smirnova, I]]
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[[Category: Smirnova I]]
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[[Category: Dna-binding]]
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[[Category: Transcription]]
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[[Category: Transcription factor]]
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[[Category: Transcription regulation]]
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[[Category: Transcription regulator]]
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Current revision

DntR Inducer Binding Domain in Complex with Salicylate. Trigonal crystal form

PDB ID 2y7p

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