View source for 6hof


==TRANSCRIPTIONAL REPRESSOR ETHR FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH BDM44852==
<StructureSection load='6hof' size='340' side='right'caption='[[6hof]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6hof]] is a 1 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=6HOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HOF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GJ8:4-[2-(phenylsulfonylaminomethyl)-1,3-thiazol-4-yl]-~{N}-[3,3,3-tris(fluoranyl)propyl]benzamide'>GJ8</scene></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=6hof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hof OCA], [https://pdbe.org/6hof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hof RCSB], [https://www.ebi.ac.uk/pdbsum/6hof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hof ProSAT]</span></td></tr>
</table>
== Function ==
[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 ==
The Mycobacterium tuberculosis EthR is a member of the TetR family of repressors, controlling the expression of EthA, a mono-oxygenase responsible for the bioactivation of the prodrug ethionamide. This protein was established as a promising therapeutic target against tuberculosis, allowing, when inhibited by a drug-like molecule, to boost the action of ethionamide. Dozens of EthR crystal structures have been solved in complex with ligands. Herein, we disclose EthR structures in complex with 18 different small molecules and then performed in-depth analysis on the complete set of EthR structures that provides insights on EthR-ligand interactions. The 81 molecules solved in complex with EthR show a large diversity of chemical structures that were split up into several chemical clusters. Two of the most striking common points of EthR-ligand interactions are the quasi-omnipresence of a hydrogen bond bridging compounds with Asn(179) and the high occurrence of pi-pi interactions involving Phe(110). A systematic analysis of the protein-ligand contacts identified eight hot spot residues that defined the basic structural features governing the binding mode of small molecules to EthR. Implications for the design of new potent inhibitors are discussed.

A comprehensive analysis of the protein-ligand interactions in crystal structures of Mycobacterium tuberculosis EthR.,Tanina A, Wohlkonig A, Soror SH, Flipo M, Villemagne B, Prevet H, Deprez B, Moune M, Peree H, Meyer F, Baulard AR, Willand N, Wintjens R Biochim Biophys Acta Proteins Proteom. 2018 Dec 13. pii: S1570-9639(18)30212-7., doi: 10.1016/j.bbapap.2018.12.003. PMID:30553830<ref>PMID:30553830</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6hof" style="background-color:#fffaf0;"></div>

==See Also==
*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis CDC1551]]
[[Category: Wintjens R]]
[[Category: Wohlkonig A]]