5d1w

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==Crystal structure of Mycobacterium tuberculosis Rv3249c transcriptional regulator.==
==Crystal structure of Mycobacterium tuberculosis Rv3249c transcriptional regulator.==
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<StructureSection load='5d1w' size='340' side='right' caption='[[5d1w]], [[Resolution|resolution]] 3.59&Aring;' scene=''>
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<StructureSection load='5d1w' size='340' side='right'caption='[[5d1w]], [[Resolution|resolution]] 3.59&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5d1w]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D1W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D1W FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5d1w]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D1W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D1W FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</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]] 3.59&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d1r|5d1r]]</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=PLM:PALMITIC+ACID'>PLM</scene></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=5d1w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d1w OCA], [http://pdbe.org/5d1w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d1w RCSB], [http://www.ebi.ac.uk/pdbsum/5d1w PDBsum]</span></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=5d1w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d1w OCA], [https://pdbe.org/5d1w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d1w RCSB], [https://www.ebi.ac.uk/pdbsum/5d1w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d1w 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/O05892_MYCTU O05892_MYCTU]
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Mycobacterium tuberculosis is a pathogenic bacterial species, which is neither Gram positive nor Gram negative. It has a unique cell wall, making it difficult to kill and conferring resistance to antibiotics that disrupt cell wall biosynthesis. Thus, the mycobacterial cell wall is critical to the virulence of these pathogens. Recent work shows that the mycobacterial membrane protein large (MmpL) family of transporters contributes to cell wall biosynthesis by exporting fatty acids and lipidic elements of the cell wall. The expression of the Mycobacterium tuberculosis MmpL proteins is controlled by a complicated regulatory network system. Here we report crystallographic structures of two forms of the TetR-family transcriptional regulator Rv0302, which participates in regulating the expression of MmpL proteins. The structures reveal a dimeric, two-domain molecule with architecture consistent with the TetR family of regulators. Comparison of the two Rv0302 crystal structures suggests that the conformational changes leading to derepression may be due to a rigid body rotational motion within the dimer interface of the regulator. Using fluorescence polarization and electrophoretic mobility shift assays, we demonstrate the recognition of promoter and intragenic regions of multiple mmpL genes by this protein. In addition, our isothermal titration calorimetry and electrophoretic mobility shift experiments indicate that fatty acids may be the natural ligand of this regulator. Taken together, these experiments provide new perspectives on the regulation of the MmpL family of transporters.
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Crystal structure of the Mycobacterium tuberculosis transcriptional regulator Rv0302.,Chou TH, Delmar JA, Wright CC, Kumar N, Radhakrishnan A, Doh JK, Licon MH, Bolla JR, Lei HT, Rajashankar KR, Su CC, Purdy GE, Yu EW Protein Sci. 2015 Sep 12. doi: 10.1002/pro.2802. PMID:26362239<ref>PMID:26362239</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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==See Also==
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</div>
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*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]]
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<div class="pdbe-citations 5d1w" 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: Chou, T H]]
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[[Category: Large Structures]]
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[[Category: Delmar, J]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Su, C C]]
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[[Category: Chou T-H]]
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[[Category: Yu, E]]
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[[Category: Delmar J]]
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Su C-C]]
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[[Category: Transcription]]
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[[Category: Yu E]]
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[[Category: Transcriptional regulator]]
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Current revision

Crystal structure of Mycobacterium tuberculosis Rv3249c transcriptional regulator.

PDB ID 5d1w

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