1jus: Difference between revisions
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==Crystal structure of the multidrug binding transcriptional repressor QacR bound to rhodamine 6G== | ==Crystal structure of the multidrug binding transcriptional repressor QacR bound to rhodamine 6G== | ||
<StructureSection load='1jus' size='340' side='right' caption='[[1jus]], [[Resolution|resolution]] 2.84Å' scene=''> | <StructureSection load='1jus' size='340' side='right' caption='[[1jus]], [[Resolution|resolution]] 2.84Å' scene=''> | ||
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<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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jt0|1jt0]], [[1jt6|1jt6]], [[1jtx|1jtx]], [[1jty|1jty]], [[1jum|1jum]], [[1jup|1jup]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jt0|1jt0]], [[1jt6|1jt6]], [[1jtx|1jtx]], [[1jty|1jty]], [[1jum|1jum]], [[1jup|1jup]]</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=1jus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jus OCA], [http://pdbe.org/1jus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jus RCSB], [http://www.ebi.ac.uk/pdbsum/1jus PDBsum]</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=1jus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jus OCA], [http://pdbe.org/1jus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jus RCSB], [http://www.ebi.ac.uk/pdbsum/1jus PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jus ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ju/1jus_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ju/1jus_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> |
Revision as of 12:18, 17 January 2018
Crystal structure of the multidrug binding transcriptional repressor QacR bound to rhodamine 6GCrystal structure of the multidrug binding transcriptional repressor QacR bound to rhodamine 6G
Structural highlights
Function[QACR_STAAU] Transcriptional repressor of qacA. Binds to IR1, an unusually long 28 bp operator, which is located downstream from the qacA promoter and overlaps its transcription start site. QacR is induced from its IR1 site by binding to one of many structurally dissimilar cationic lipophilic compounds, which are also substrates of QacA. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe Staphylococcus aureus multidrug binding protein QacR represses transcription of the qacA multidrug transporter gene and is induced by structurally diverse cationic lipophilic drugs. Here, we report the crystal structures of six QacR-drug complexes. Compared to the DNA bound structure, drug binding elicits a coil-to-helix transition that causes induction and creates an expansive multidrug-binding pocket, containing four glutamates and multiple aromatic and polar residues. These structures indicate the presence of separate but linked drug-binding sites within a single protein. This multisite drug-binding mechanism is consonant with studies on multidrug resistance transporters. Structural mechanisms of QacR induction and multidrug recognition.,Schumacher MA, Miller MC, Grkovic S, Brown MH, Skurray RA, Brennan RG Science. 2001 Dec 7;294(5549):2158-63. PMID:11739955[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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