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==Crystal structure of Mycobacterium tuberculosis Rv1816 transcriptional regulator.==
==Crystal structure of Mycobacterium tuberculosis Rv1816 transcriptional regulator.==
<StructureSection load='5d1r' size='340' side='right' caption='[[5d1r]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='5d1r' size='340' side='right'caption='[[5d1r]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5d1r]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D1R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D1R FirstGlance]. <br>
<table><tr><td colspan='2'>[[5d1r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_CDC1551 Mycobacterium tuberculosis CDC1551]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D1R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D1R FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=56S:PROPAN-2-YL+DODECANOATE'>56S</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</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&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d1w|5d1w]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=56S:PROPAN-2-YL+DODECANOATE'>56S</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<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=5d1r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d1r OCA], [http://pdbe.org/5d1r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d1r RCSB], [http://www.ebi.ac.uk/pdbsum/5d1r PDBsum]</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=5d1r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d1r OCA], [https://pdbe.org/5d1r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d1r RCSB], [https://www.ebi.ac.uk/pdbsum/5d1r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d1r ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Y1816_MYCTU Y1816_MYCTU] May participate in the regulatory network that controls the expression of MmpL lipid transporters (PubMed:26396194). Binds to intragenic and/or promoter regions of rv1816, mmpL3, rv0204, mmpL11, mmpL7, kasA and mmpS3 (PubMed:26396194).<ref>PMID:26396194</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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.
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 complex regulatory network, including the TetR-family transcriptional regulators Rv3249c and Rv1816. Here we report the crystal structures of these two regulators, revealing dimeric, two-domain molecules with architecture consistent with the TetR family of regulators. Buried extensively within the C-terminal regulatory domains of Rv3249c and Rv1816 we found fortuitous bound ligands, which were identified as palmitic acid (a fatty acid) and isopropyl laurate (a fatty acid ester), respectively. Our results suggest that fatty acids may be the natural ligands of these regulatory proteins. Using fluorescence polarization and electrophoretic mobility shift assays, we demonstrate the recognition of promoter and intragenic regions of multiple mmpL genes by these proteins. Binding of palmitic acid renders these regulators incapable of interacting with their respective operator DNAs, which will result in derepression of the corresponding mmpL genes. Taken together, these experiments provide new perspectives on the regulation of the MmpL family of transporters.


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>
Structural Basis for the Regulation of the MmpL Transporters of Mycobacterium tuberculosis.,Delmar JA, Chou TH, Wright CC, Licon MH, Doh JK, Radhakrishnan A, Kumar N, Lei HT, Bolla JR, Rajashankar KR, Su CC, Purdy GE, Yu EW J Biol Chem. 2015 Sep 22. pii: jbc.M115.683797. PMID:26396194<ref>PMID:26396194</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 5d1r" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5d1r" style="background-color:#fffaf0;"></div>
==See Also==
*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Chou, T H]]
[[Category: Large Structures]]
[[Category: Delmar, J]]
[[Category: Mycobacterium tuberculosis CDC1551]]
[[Category: Su, C C]]
[[Category: Chou T-H]]
[[Category: Yu, E]]
[[Category: Delmar J]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Su C-C]]
[[Category: Transcription]]
[[Category: Yu E]]
[[Category: Transcriptional regulator]]
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