3v6g

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==Crystal Structure of Transcriptional Regulator==
==Crystal Structure of Transcriptional Regulator==
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<StructureSection load='3v6g' size='340' side='right' caption='[[3v6g]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
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<StructureSection load='3v6g' size='340' side='right'caption='[[3v6g]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3v6g]] is a 2 chain structure with sequence from [http://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=3V6G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3V6G FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3v6g]] 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=3V6G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V6G FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3v78|3v78]]</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]] 1.821&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MT3151, Rv3066 ([http://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=3v6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v6g OCA], [https://pdbe.org/3v6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v6g RCSB], [https://www.ebi.ac.uk/pdbsum/3v6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v6g ProSAT]</span></td></tr>
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<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=3v6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v6g OCA], [http://pdbe.org/3v6g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3v6g RCSB], [http://www.ebi.ac.uk/pdbsum/3v6g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3v6g ProSAT]</span></td></tr>
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</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 3v6g" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bolla, J R]]
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[[Category: Large Structures]]
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[[Category: Chen, X]]
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Do, S V]]
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[[Category: Bolla JR]]
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[[Category: Yu, E W]]
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[[Category: Chen X]]
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[[Category: Helix-turn-helix dna binding domain]]
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[[Category: Do SV]]
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[[Category: Transcription]]
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[[Category: Yu EW]]

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Crystal Structure of Transcriptional Regulator

PDB ID 3v6g

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