5ebv

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m (Protected "5ebv" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5ebv is ON HOLD until Paper Publication
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==Crystal structure of acetyltransferase Eis from Mycobacterium tuberculosis in complex with inhibitor 11c and CoA==
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<StructureSection load='5ebv' size='340' side='right' caption='[[5ebv]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5ebv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EBV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EBV 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=5LR:5-(4-CHLOROPHENYL)-~{N}-[3-(3,4-DIHYDRO-1~{H}-ISOQUINOLIN-2-YL)PROPYL]-4-METHYL-1,1-BIS(OXIDANYLIDENE)-1,2-THIAZOL-3-AMINE'>5LR</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ec4|5ec4]]</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=5ebv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ebv OCA], [http://pdbe.org/5ebv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ebv RCSB], [http://www.ebi.ac.uk/pdbsum/5ebv PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/EIS_MYCTU EIS_MYCTU]] May participate in pathogenesis, possibly by enhancing survival of the bacteria in host macrophages during infection.<ref>PMID:10629183</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A major cause of tuberculosis (TB) resistance to the aminoglycoside kanamycin (KAN) is the Mycobacterium tuberculosis (Mtb) acetyltransferase Eis. Upregulation of this enzyme is responsible for inactivation of KAN through acetylation of its amino groups. A 123000-compound high-throughput screen (HTS) yielded several small-molecule Eis inhibitors that share an isothiazole S,S-dioxide heterocyclic core. These were investigated for their structure-activity relationships. Crystal structures of Eis in complex with two potent inhibitors show that these molecules are bound in the conformationally adaptable aminoglycoside binding site of the enzyme, thereby obstructing binding of KAN for acetylation. Importantly, we demonstrate that several Eis inhibitors, when used in combination with KAN against resistant Mtb, efficiently overcome KAN resistance. This approach paves the way toward development of novel combination therapies against aminoglycoside-resistant TB.
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Authors: Gajadeera, C.S., Hou, C., Garneau-Tsodikova, S., Tsodikov, O.V.
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Potent Inhibitors of Acetyltransferase Eis Overcome Kanamycin Resistance in Mycobacterium tuberculosis.,Willby MJ, Green KD, Gajadeera CS, Hou C, Tsodikov OV, Posey JE, Garneau-Tsodikova S ACS Chem Biol. 2016 Apr 7. PMID:27010218<ref>PMID:27010218</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Tsodikov, O.V]]
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<div class="pdbe-citations 5ebv" style="background-color:#fffaf0;"></div>
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[[Category: Hou, C]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Gajadeera, C S]]
[[Category: Garneau-Tsodikova, S]]
[[Category: Garneau-Tsodikova, S]]
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[[Category: Gajadeera, C.S]]
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[[Category: Hou, C]]
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[[Category: Tsodikov, O V]]
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[[Category: Aminoglycoside]]
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[[Category: Resistance]]
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[[Category: Transferase]]
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[[Category: Transferase-transferase inhibitor complex]]
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[[Category: Tuberculosis]]

Revision as of 16:33, 10 May 2016

Crystal structure of acetyltransferase Eis from Mycobacterium tuberculosis in complex with inhibitor 11c and CoA

5ebv, resolution 2.20Å

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