7ag8: Difference between revisions

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-'''Unreleased structure'''
-The entry 7ag8 is ON HOLD  until Paper Publication
+==Cryo-EM structure of wild-type KatG from M. tuberculosis==
+<StructureSection load='7ag8' size='340' side='right'caption='[[7ag8]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AG8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AG8 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.68&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=7ag8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ag8 OCA], [https://pdbe.org/7ag8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ag8 RCSB], [https://www.ebi.ac.uk/pdbsum/7ag8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ag8 ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Resolution advances in cryoelectron microscopy (cryo-EM) now offer the possibility to visualize structural effects of naturally occurring resistance mutations in proteins and also of understanding the binding mechanisms of small drug molecules. In Mycobacterium tuberculosis the multifunctional heme enzyme KatG is indispensable for activation of isoniazid (INH), a first-line pro-drug for treatment of tuberculosis. We present a cryo-EM methodology for structural and functional characterization of KatG and INH resistance variants. The cryo-EM structure of the 161 kDa KatG dimer in the presence of INH is reported to 2.7 A resolution allowing the observation of potential INH binding sites. In addition, cryo-EM structures of two INH resistance variants, identified from clinical isolates, W107R and T275P, are reported. In combination with electronic absorbance spectroscopy our cryo-EM approach reveals how these resistance variants cause disorder in the heme environment preventing heme uptake and retention, providing insight into INH resistance.
-Authors: Blundell, T.L., Chaplin, A.K., Munir, A.
+Using cryo-EM to understand antimycobacterial resistance in the catalase-peroxidase (KatG) from Mycobacterium tuberculosis.,Munir A, Wilson MT, Hardwick SW, Chirgadze DY, Worrall JAR, Blundell TL, Chaplin AK Structure. 2021 Jan 4. pii: S0969-2126(20)30475-5. doi:, 10.1016/j.str.2020.12.008. PMID:33444527<ref>PMID:33444527</ref>
-Description: Cryo-EM structure of wild-type KatG from M. tuberculosis
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Blundell, T.L]]
+<div class="pdbe-citations 7ag8" style="background-color:#fffaf0;"></div>
-[[Category: Chaplin, A.K]]
-[[Category: Munir, A]]
+==See Also==
+*[[Catalase 3D structures|Catalase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Blundell TL]]
+[[Category: Chaplin AK]]
+[[Category: Munir A]]