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3tp3

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==Structure of HTH-type transcriptional regulator EthR, G106W mutant==
==Structure of HTH-type transcriptional regulator EthR, G106W mutant==
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<StructureSection load='3tp3' size='340' side='right' caption='[[3tp3]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
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<StructureSection load='3tp3' size='340' side='right'caption='[[3tp3]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tp3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TP3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TP3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3tp3]] is a 1 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=3TP3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TP3 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tp0|3tp0]]</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]] 1.86&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ethR, etaR, MT3970, Rv3855 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])</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=3tp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tp3 OCA], [https://pdbe.org/3tp3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tp3 RCSB], [https://www.ebi.ac.uk/pdbsum/3tp3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tp3 ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tp3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tp3 RCSB], [http://www.ebi.ac.uk/pdbsum/3tp3 PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/ETHR_MYCTU ETHR_MYCTU] Involved in the repression of the monooxygenase EthA which is responsible of the formation of the active metabolite of ethionamide (ETH).<ref>PMID:10869356</ref> <ref>PMID:10944230</ref>
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== Publication Abstract from PubMed ==
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Ethionamide is an antituberculous drug for the treatment of multidrug-resistant Mycobacterium tuberculosis. This antibiotic requires activation by the monooxygenase EthA to exert its activity. Production of EthA is controlled by the transcriptional repressor EthR, a member of the TetR family. The sensitivity of M. tuberculosis to ethionamide can be artificially enhanced using synthetic ligands of EthR that allosterically inactivate its DNA-binding activity. Comparison of several structures of EthR co-crystallized with various ligands suggested that the structural reorganization of EthR resulting in its inactivation is controlled by a limited portion of the ligand-binding-pocket. In silico simulation predicted that mutation G106W may mimic ligands. X-ray crystallography of variant G106W indeed revealed a protein structurally similar to ligand-bound EthR. Surface plasmon resonance experiments established that this variant is unable to bind DNA, while thermal shift studies demonstrated that mutation G106W stabilizes EthR as strongly as ligands. Proton NMR of the methyl regions showed a lesser contribution of exchange broadening upon ligand binding, and the same quenched dynamics was observed in apo-variant G106W. Altogether, we here show that the area surrounding Gly106 constitutes the molecular switch involved in the conformational reorganization of EthR. These results also shed light on the mechanistic of ligand-induced allosterism controlling the DNA binding properties of TetR family repressors.
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Structural activation of the transcriptional repressor EthR from Mycobacterium tuberculosis by single amino acid change mimicking natural and synthetic ligands.,Carette X, Blondiaux N, Willery E, Hoos S, Lecat-Guillet N, Lens Z, Wohlkonig A, Wintjens R, Soror SH, Frenois F, Dirie B, Villeret V, England P, Lippens G, Deprez B, Locht C, Willand N, Baulard AR Nucleic Acids Res. 2011 Dec 9. PMID:22156370<ref>PMID:22156370</ref>
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From MEDLINE®/PubMed®, 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]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: Carette, Xavier.]]
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[[Category: Carette X]]
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[[Category: Tetr family]]
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[[Category: Transcription]]
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[[Category: Transcriptional regulatory repressor protein]]
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Current revision

Structure of HTH-type transcriptional regulator EthR, G106W mutant

PDB ID 3tp3

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