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| - | ==Crystal Structure of B. pseudomallei KatG treated with hydrogen peroxide==
| + | #REDIRECT [[5syk]] This PDB entry is obsolete and replaced by 5syk |
| - | <StructureSection load='4mvp' size='340' side='right' caption='[[4mvp]], [[Resolution|resolution]] 1.80Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[4mvp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MVP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MVP 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TOX:1-HYDROPEROXY-L-TRYPTOPHAN'>TOX</scene></td></tr>
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| - | <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>
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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=4mvp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mvp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mvp RCSB], [http://www.ebi.ac.uk/pdbsum/4mvp PDBsum]</span></td></tr>
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| - | </table>
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| - | == Function ==
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| - | [[http://www.uniprot.org/uniprot/B7CLB5_BURPE B7CLB5_BURPE]] Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity (By similarity).[HAMAP-Rule:MF_01961]
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Catalase peroxidases (KatG's) are bifunctional heme proteins that can disproportionate hydrogen peroxide (catalatic reaction) despite their structural dissimilarity with monofunctional catalases. Using X-ray crystallography and QM/MM calculations, we demonstrate that the catalatic reaction of KatG's involves deprotonation of the active-site Trp, which plays a role similar to that of the distal His in monofunctional catalases. The interaction of a nearby mobile arginine with the distal Met-Tyr-Trp essential adduct (in/out) acts as an electronic switch, triggering deprotonation of the adduct Trp.
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| - | An ionizable active-site tryptophan imparts catalase activity to a peroxidase core.,Loewen PC, Carpena X, Vidossich P, Fita I, Rovira C J Am Chem Soc. 2014 May 21;136(20):7249-52. doi: 10.1021/ja502794e. Epub 2014 May, 7. PMID:24785434<ref>PMID:24785434</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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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: Catalase peroxidase]]
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| - | [[Category: Carpena, X]]
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| - | [[Category: Fita, I]]
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| - | [[Category: Loewen, P C]]
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| - | [[Category: Catalase-peroxidase]]
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| - | [[Category: Hydrogen peroxide]]
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| - | [[Category: Inh]]
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| - | [[Category: Oxidoreductase]]
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| - | [[Category: Peroxidase-like core]]
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