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4mvp
From Proteopedia
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| - | ''' | + | ==Crystal Structure of B. pseudomallei KatG treated with hydrogen peroxide== |
| + | <StructureSection load='4mvp' size='340' side='right' caption='[[4mvp]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </td></tr><tr><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><br> | ||
| + | <tr><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> | ||
| + | <tr><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><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> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Catalase peroxidase]] | ||
| + | [[Category: Carpena, X.]] | ||
| + | [[Category: Fita, I.]] | ||
| + | [[Category: Loewen, P C.]] | ||
| + | [[Category: Catalase-peroxidase]] | ||
| + | [[Category: Hydrogen peroxide]] | ||
| + | [[Category: Inh]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Peroxidase-like core]] | ||
Revision as of 02:25, 7 August 2014
Crystal Structure of B. pseudomallei KatG treated with hydrogen peroxide
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