1r8d

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[[Image:1r8d.gif|left|200px]]
 
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==Crystal Structure of MtaN Bound to DNA==
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The line below this paragraph, containing "STRUCTURE_1r8d", creates the "Structure Box" on the page.
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<StructureSection load='1r8d' size='340' side='right'caption='[[1r8d]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1r8d]] is a 4 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=1R8D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R8D FirstGlance]. <br>
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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]] 2.7&#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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1r8d| PDB=1r8d | SCENE= }}
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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=1r8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r8d OCA], [https://pdbe.org/1r8d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r8d RCSB], [https://www.ebi.ac.uk/pdbsum/1r8d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r8d ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MTA_BACSU MTA_BACSU] Global transcriptional regulator that activates transcription of bmr and blt by binding directly to their promoter. Stimulates also the expression of the mta gene itself, ydfK and ymfE.<ref>PMID:10200972</ref> <ref>PMID:18502870</ref>
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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/r8/1r8d_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=1r8d ConSurf].
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<div style="clear:both"></div>
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'''Crystal Structure of MtaN Bound to DNA'''
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==See Also==
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*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
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== References ==
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==Overview==
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<references/>
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Transcription regulators of the MerR family respond to myriad stress signals to activate sigma70/sigmaA-targeted genes, which contain suboptimal 19-bp spacers between their -35 and -10 promoter elements. The crystal structure of a BmrR-TPP(+)-DNA complex provided initial insight into the transcription activation mechanism of the MerR family, which involves base pair distortion, DNA undertwisting and shortening of the spacer, and realignment of the -35 and -10 boxes. Here, we describe the crystal structure of MerR family member MtaN bound to the mta promoter. Although the global DNA binding modes of MtaN and BmrR differ somewhat, homologous protein-DNA interactions are maintained. Moreover, despite their different sequences, the mta promoter conformation is essentially identical to that of the BmrR-TPP(+)-bound bmr promoter, indicating that this DNA distortion mechanism is common to the entire MerR family. Interestingly, DNA binding experiments reveal that the identity of the two central bases of the mta and bmr promoters, which are conserved as either a thymidine or an adenine in nearly all MerR promoters, is not important for DNA affinity. Comparison of the free and DNA-bound MtaN structures reveals that a conformational hinge, centered at residues N-terminal to the ubiquitous coiled coil, is key for mta promoter binding. Analysis of the structures of BmrR, CueR, and ZntR indicates that this hinge may be common to all MerR family members.
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__TOC__
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</StructureSection>
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==About this Structure==
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1R8D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R8D OCA].
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==Reference==
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The structural mechanism for transcription activation by MerR family member multidrug transporter activation, N terminus., Newberry KJ, Brennan RG, J Biol Chem. 2004 May 7;279(19):20356-62. Epub 2004 Feb 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14985361 14985361]
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[[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: Newberry, K J.]]
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[[Category: Newberry KJ]]
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[[Category: Protein-dna complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:12:45 2008''
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Current revision

Crystal Structure of MtaN Bound to DNA

PDB ID 1r8d

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