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| | ==Crystal structure of BmrR bound to puromycin== | | ==Crystal structure of BmrR bound to puromycin== |
| - | <StructureSection load='3q3d' size='340' side='right' caption='[[3q3d]], [[Resolution|resolution]] 2.79Å' scene=''> | + | <StructureSection load='3q3d' size='340' side='right'caption='[[3q3d]], [[Resolution|resolution]] 2.79Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3q3d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] and [http://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 [http://oca.weizmann.ac.il/oca-docs/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"><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]] 2.79Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3d6y|3d6y]], [[3d6z|3d6z]]</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 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3q3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q3d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q3d RCSB], [http://www.ebi.ac.uk/pdbsum/3q3d PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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;">
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| - | == Publication Abstract from PubMed ==
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| - | 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.
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| - | 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>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | == References ==
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| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Bacillus subtilis]] | | [[Category: Bacillus subtilis]] |
| - | [[Category: Streptomyces alboniger]] | + | [[Category: Large Structures]] |
| - | [[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]]
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| - | [[Category: Multi-drug binding]]
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| - | [[Category: Protein-dna complex]]
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| - | [[Category: Transcription regulator]]
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| - | [[Category: Transcription regulator-dna-antibiotic complex]]
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