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3q3d

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Crystal structure of BmrR bound to puromycin

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@@ Line 3: / Line 3: @@
 <StructureSection load='3q3d' size='340' side='right'caption='[[3q3d]], [[Resolution|resolution]] 2.79&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3q3d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835] and [https://en.wikipedia.org/wiki/Streptomyces_alboniger Streptomyces alboniger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q3D FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3q3d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q3D FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PUY:PUROMYCIN'>PUY</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]] 2.79&#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;'>[[3d6y|3d6y]], [[3d6z|3d6z]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PUY:PUROMYCIN'>PUY</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bmrR, bmr1R, BSU24020 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</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=3q3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q3d OCA], [https://pdbe.org/3q3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q3d RCSB], [https://www.ebi.ac.uk/pdbsum/3q3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q3d ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/BMRR_BACSU BMRR_BACSU]] Activates transcription of the bmr gene in response to structurally dissimilar drugs. Binds rhodamine as an inducer.
+[https://www.uniprot.org/uniprot/BMRR_BACSU BMRR_BACSU] Activates transcription of the bmr gene in response to structurally dissimilar drugs. Binds rhodamine as an inducer.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Current views of multidrug (MD) recognition focus on large drug-binding cavities with flexible elements. However, MD recognition in BmrR is supported by a small, rigid drug-binding pocket. Here, a detailed description of MD binding by the noncanonical BmrR protein is offered through the combined use of X-ray and solution studies. Low shape complementarity, suboptimal packing, and efficient burial of a diverse set of ligands is facilitated by an aromatic docking platform formed by a set of conformationally fixed aromatic residues, hydrophobic pincer pair that locks the different drug structures on the adaptable platform surface, and a trio of acidic residues that enables cation selectivity without much regard to ligand structure. Within the binding pocket is a set of BmrR-derived H-bonding donor and acceptors that solvate a wide range of ligand polar substituent arrangements in a manner analogous to aqueous solvent. Energetic analyses of MD binding by BmrR are consistent with structural data. A common binding orientation for the different BmrR ligands is in line with promiscuous allosteric regulation.
-Structural contributions to multidrug recognition in the multidrug resistance (MDR) gene regulator, BmrR.,Bachas S, Eginton C, Gunio D, Wade H Proc Natl Acad Sci U S A. 2011 Jul 5;108(27):11046-51. Epub 2011 Jun 20. PMID:21690368<ref>PMID:21690368</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3q3d" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Vibrio subtilis ehrenberg 1835]]
+[[Category: Bacillus subtilis]]
 [[Category: Large Structures]]
-[[Category: Streptomyces alboniger]]
+[[Category: Bachas S]]
-[[Category: Bachas, S]]
+[[Category: Eginton C]]
-[[Category: Eginton, C]]
+[[Category: Gunio G]]
-[[Category: Gunio, G]]
+[[Category: Wade H]]
-[[Category: Wade, H]]
-[[Category: Antibiotic]]
-[[Category: Multi-drug binding]]
-[[Category: Protein-dna complex]]
-[[Category: Transcription regulator]]
-[[Category: Transcription regulator-dna-antibiotic complex]]

3q3d

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Crystal structure of BmrR bound to puromycin

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