This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3q0w

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

ETHR From mycobacterium tuberculosis in complex with compound BDM33066

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3q0w"

@@ Line 1: / Line 1: @@
 ==ETHR From mycobacterium tuberculosis in complex with compound BDM33066==
-<StructureSection load='3q0w' size='340' side='right' caption='[[3q0w]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+<StructureSection load='3q0w' size='340' side='right'caption='[[3q0w]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3q0w]] 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=3Q0W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q0W FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3q0w]] 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=3Q0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q0W FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LL5:(2S)-2-AMINO-3-METHYL-1-{4-[3-(THIOPHEN-2-YL)-1,2,4-OXADIAZOL-5-YL]PIPERIDIN-1-YL}BUTAN-1-ONE'>LL5</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]] 1.6&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o8g|3o8g]], [[3o8l|3o8l]], [[3g1m|3g1m]], [[3g1l|3g1l]], [[3g1o|3g1o]], [[1u9n|1u9n]], [[3q0u|3q0u]], [[3q0v|3q0v]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LL5:(2S)-2-AMINO-3-METHYL-1-{4-[3-(THIOPHEN-2-YL)-1,2,4-OXADIAZOL-5-YL]PIPERIDIN-1-YL}BUTAN-1-ONE'>LL5</scene></td></tr>
-<tr id='gene'><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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3q0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q0w OCA], [https://pdbe.org/3q0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q0w RCSB], [https://www.ebi.ac.uk/pdbsum/3q0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q0w ProSAT]</span></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=3q0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q0w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q0w RCSB], [http://www.ebi.ac.uk/pdbsum/3q0w PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[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>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+==See Also==
-</div>
+*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Mycobacterium tuberculosis]]
-[[Category: Baulard, A]]
+[[Category: Baulard A]]
-[[Category: Brodin, P]]
+[[Category: Brodin P]]
-[[Category: Carette, X]]
+[[Category: Carette X]]
-[[Category: Christophe, T]]
+[[Category: Christophe T]]
-[[Category: Demirkaya, F]]
+[[Category: Demirkaya F]]
-[[Category: Deprez, B]]
+[[Category: Deprez B]]
-[[Category: Desrose, M]]
+[[Category: Desrose M]]
-[[Category: Dirie, B]]
+[[Category: Dirie B]]
-[[Category: Flipo, M]]
+[[Category: Flipo M]]
-[[Category: Jeon, H K]]
+[[Category: Jeon HK]]
-[[Category: Lens, Z]]
+[[Category: Lens Z]]
-[[Category: Leroux, F]]
+[[Category: Leroux F]]
-[[Category: Locht, C]]
+[[Category: Locht C]]
-[[Category: Piveteau, C]]
+[[Category: Piveteau C]]
-[[Category: Rucktooa, P]]
+[[Category: Rucktooa P]]
-[[Category: Villeret, V]]
+[[Category: Villeret V]]
-[[Category: Willand, N]]
+[[Category: Willand N]]
-[[Category: Tetr family]]
-[[Category: Transcription-transcription inhibitor complex]]
-[[Category: Transcriptional repressor]]

3q0w

From Proteopedia

Current revision

ETHR From mycobacterium tuberculosis in complex with compound BDM33066

Structural highlights

Function

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox