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3v78

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Current revision (14:19, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3v78' size='340' side='right'caption='[[3v78]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3v78' size='340' side='right'caption='[[3v78]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3v78]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V78 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V78 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3v78]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V78 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V78 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ET:ETHIDIUM'>ET</scene></td></tr>
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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]] 2.299&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3v6g|3v6g]]</div></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=ET:ETHIDIUM'>ET</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MT3151, Rv3066 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr>
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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=3v78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v78 OCA], [https://pdbe.org/3v78 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v78 RCSB], [https://www.ebi.ac.uk/pdbsum/3v78 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v78 ProSAT]</span></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=3v78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v78 OCA], [https://pdbe.org/3v78 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v78 RCSB], [https://www.ebi.ac.uk/pdbsum/3v78 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v78 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/P95092_MYCTO P95092_MYCTO]
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The Mmr multidrug efflux pump recognizes and actively extrudes a broad range of antimicrobial agents, and promotes the intrinsic resistance to these antimicrobials in Mycobacterium tuberculosis. The expression of Mmr is controlled by the TetR-like transcriptional regulator Rv3066, whose open reading frame is located downstream of the mmr operon. To understand the structural basis of Rv3066 regulation, we have determined the crystal structures of Rv3066, both in the absence and presence of bound ethidium, revealing an asymmetric homodimeric two-domain molecule with an entirely helical architecture. The structures underscore the flexibility and plasticity of the regulator essential for multidrug recognition. Comparison of the apo-Rv3066 and Rv3066-ethidium crystal structures suggests that the conformational changes leading to drug-mediated derepression is primarily due to a rigid body rotational motion within the dimer interface of the regulator. The Rv3066 regulator creates a multidrug-binding pocket, which contains five aromatic residues. The bound ethidium is found buried within the multidrug-binding site, where extensive aromatic stacking interactions seemingly govern the binding. In vitro studies reveal that the dimeric Rv3066 regulator binds to a 14-bp palindromic inverted repeat sequence in the nanomolar range. These findings provide new insight into the mechanisms of ligand binding and Rv3066 regulation.
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Structural and functional analysis of the transcriptional regulator Rv3066 of Mycobacterium tuberculosis.,Bolla JR, Do SV, Long F, Dai L, Su CC, Lei HT, Chen X, Gerkey JE, Murphy DC, Rajashankar KR, Zhang Q, Yu EW Nucleic Acids Res. 2012 Jul 19. PMID:22821564<ref>PMID:22821564</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3v78" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bolla, J R]]
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Chen, X]]
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[[Category: Bolla JR]]
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[[Category: Do, S V]]
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[[Category: Chen X]]
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[[Category: Yu, E W]]
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[[Category: Do SV]]
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[[Category: Helix-turn-helix dna binding domain]]
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[[Category: Yu EW]]
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[[Category: Transcription]]
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Current revision

Crystal Structure of Transcriptional Regulator

PDB ID 3v78

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