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1exi

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(New page: 200px<br /><applet load="1exi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1exi, resolution 3.12&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1exi.gif|left|200px]]<br /><applet load="1exi" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1exi, resolution 3.12&Aring;" />
 
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'''CRYSTAL STRUCTURE OF TRANSCRIPTION ACTIVATOR BMRR, FROM B. SUBTILIS, BOUND TO 21 BASE PAIR BMR OPERATOR AND TPSB'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF TRANSCRIPTION ACTIVATOR BMRR, FROM B. SUBTILIS, BOUND TO 21 BASE PAIR BMR OPERATOR AND TPSB==
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The efflux of chemically diverse drugs by multidrug transporters that span, the membrane is one mechanism of multidrug resistance in bacteria. The, concentrations of many of these transporters are controlled by, transcription regulators, such as BmrR in Bacillus subtilis, EmrR in, Escherichia coli and QacR in Staphylococcus aureus. These proteins promote, transporter gene expression when they bind toxic compounds. BmrR activates, transcription of the multidrug transporter gene, bmr, in response to, cellular invasion by certain lipophilic cationic compounds (drugs). BmrR, belongs to the MerR family, which regulates response to stress such as, exposure to toxic compounds or oxygen radicals in bacteria. MerR proteins, have homologous amino-terminal DNA-binding domains but different, carboxy-terminal domains, which enable them to bind specific 'coactivator', molecules. When bound to coactivator, MerR proteins upregulate, transcription by reconfiguring the 19-base-pair spacer found between the, -35 and -10 promoter elements to allow productive interaction with RNA, polymerase. Here we report the 3.0 A resolution structure of BmrR in, complex with the drug tetraphenylphosphonium (TPP) and a 22-base-pair, oligodeoxynucleotide encompassing the bmr promoter. The structure reveals, an unexpected mechanism for transcription activation that involves, localized base-pair breaking, and base sliding and realignment of the -35, and -10 operator elements.
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<StructureSection load='1exi' size='340' side='right'caption='[[1exi]], [[Resolution|resolution]] 3.12&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1exi]] 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=1EXI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EXI FirstGlance]. <br>
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1EXI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with ZN and 118 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EXI OCA].
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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]] 3.12&#8491;</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=118:TETRAPHENYLANTIMONIUM+ION'>118</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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==Reference==
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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=1exi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1exi OCA], [https://pdbe.org/1exi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1exi RCSB], [https://www.ebi.ac.uk/pdbsum/1exi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1exi ProSAT]</span></td></tr>
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Crystal structure of the transcription activator BmrR bound to DNA and a drug., Heldwein EE, Brennan RG, Nature. 2001 Jan 18;409(6818):378-82. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11201751 11201751]
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ex/1exi_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1exi ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Brennan, R.G.]]
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[[Category: Brennan RG]]
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[[Category: Zheleznova-Heldwein, E.E.]]
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[[Category: Zheleznova-Heldwein EE]]
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[[Category: 118]]
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[[Category: ZN]]
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[[Category: merr-family transcription activator]]
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[[Category: multidrug-binding protein]]
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[[Category: protein-dna complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:24:13 2007''
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Current revision

CRYSTAL STRUCTURE OF TRANSCRIPTION ACTIVATOR BMRR, FROM B. SUBTILIS, BOUND TO 21 BASE PAIR BMR OPERATOR AND TPSB

PDB ID 1exi

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