4c50: Difference between revisions

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 <StructureSection load='4c50' size='340' side='right'caption='[[4c50]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4c50]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C50 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C50 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4c50]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C50 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C50 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c51|4c51]]</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=4c50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c50 OCA], [https://pdbe.org/4c50 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c50 RCSB], [https://www.ebi.ac.uk/pdbsum/4c50 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c50 ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Catalase_peroxidase Catalase peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.21 1.11.1.21] </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=4c50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c50 OCA], [http://pdbe.org/4c50 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c50 RCSB], [http://www.ebi.ac.uk/pdbsum/4c50 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c50 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/KATG_MYCTU KATG_MYCTU]] Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, isoniazid (INH) lyase and isonicotinoyl-NAD synthase activity. May play a role in the intracellular survival of mycobacteria. May be involved in DNA repair. Partly complements recA-deficient E.coli cells exposed to UV radiation, mitomycin C or hydrogen peroxide. Increases resistance to mitomycin C in E.coli cells deficient for either uvrA, uvrB or uvrC.<ref>PMID:10463167</ref>
+[[https://www.uniprot.org/uniprot/KATG_MYCTU KATG_MYCTU]] Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, isoniazid (INH) lyase and isonicotinoyl-NAD synthase activity. May play a role in the intracellular survival of mycobacteria. May be involved in DNA repair. Partly complements recA-deficient E.coli cells exposed to UV radiation, mitomycin C or hydrogen peroxide. Increases resistance to mitomycin C in E.coli cells deficient for either uvrA, uvrB or uvrC.<ref>PMID:10463167</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Peroxidatic activation of the anti-tuberculosis pro-drug isoniazid by Mycobacterium tuberculosis catalase-peroxidase (KatG) is regulated by gating residues of a heme access channel. The steric restriction at the bottleneck of this channel is alleviated by replacement of residue Asp137 with Ser, according to crystallographic and kinetic studies.
-Access channel residues Ser315 and Asp137 in Mycobacterium tuberculosis catalase-peroxidase (KatG) control peroxidatic activation of the pro-drug isoniazid.,Zhao X, Hersleth HP, Zhu J, Andersson KK, Magliozzo RS Chem Commun (Camb). 2013 Nov 4. PMID:24185282<ref>PMID:24185282</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4c50" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 27: / Line 16: @@
 __TOC__
 </StructureSection>
-[[Category: Catalase peroxidase]]
 [[Category: Large Structures]]
-[[Category: Myctu]]
+[[Category: Mycobacterium tuberculosis H37Rv]]
-[[Category: Andersson, K K]]
+[[Category: Andersson KK]]
-[[Category: Hersleth, H P]]
+[[Category: Hersleth H-P]]
-[[Category: Magliozzo, R S]]
+[[Category: Magliozzo RS]]
-[[Category: Zhao, X]]
+[[Category: Zhao X]]
-[[Category: Oxidoreductase]]