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| | ==Crystal Structure of Eukaryotic Oxoiron MagKatG2 at pH 8.5== | | ==Crystal Structure of Eukaryotic Oxoiron MagKatG2 at pH 8.5== |
| - | <StructureSection load='5cjh' size='340' side='right' caption='[[5cjh]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='5cjh' size='340' side='right'caption='[[5cjh]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5cjh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mago7 Mago7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CJH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CJH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5cjh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyricularia_oryzae_70-15 Pyricularia oryzae 70-15]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CJH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=522:PEROXIDIZED+HEME'>522</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ut2|3ut2]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=522:PEROXIDIZED+HEME'>522</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KATG2, CPXB, MagKatG2, MGG_09834 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=242507 MAGO7])</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=5cjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cjh OCA], [https://pdbe.org/5cjh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cjh RCSB], [https://www.ebi.ac.uk/pdbsum/5cjh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cjh 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=5cjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cjh OCA], [http://pdbe.org/5cjh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cjh RCSB], [http://www.ebi.ac.uk/pdbsum/5cjh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cjh ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/KATG2_MAGO7 KATG2_MAGO7]] Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Confers resistance to H(2)O(2) in hyphae. May play an antioxidative role in fungal defense against the host-produced H(2)O(2) (oxidative burst) at the early stage of plant infection.<ref>PMID:21043575</ref> <ref>PMID:21971530</ref> | + | [https://www.uniprot.org/uniprot/KATG2_MAGO7 KATG2_MAGO7] Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Confers resistance to H(2)O(2) in hyphae. May play an antioxidative role in fungal defense against the host-produced H(2)O(2) (oxidative burst) at the early stage of plant infection.<ref>PMID:21043575</ref> <ref>PMID:21971530</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Catalase|Catalase]] | + | *[[Catalase 3D structures|Catalase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Catalase peroxidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Mago7]] | + | [[Category: Pyricularia oryzae 70-15]] |
| - | [[Category: Carpena, X]] | + | [[Category: Carpena X]] |
| - | [[Category: Fita, I]] | + | [[Category: Fita I]] |
| - | [[Category: Gasselhuber, B]] | + | [[Category: Gasselhuber B]] |
| - | [[Category: Obinger, C]] | + | [[Category: Obinger C]] |
| - | [[Category: Compound i]]
| + | |
| - | [[Category: Oxidoreductase]]
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| - | [[Category: Oxoiron catalase-peroxidase]]
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| Structural highlights
Function
KATG2_MAGO7 Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Confers resistance to H(2)O(2) in hyphae. May play an antioxidative role in fungal defense against the host-produced H(2)O(2) (oxidative burst) at the early stage of plant infection.[1] [2]
Publication Abstract from PubMed
Recently, it was demonstrated that bifunctional catalase-peroxidases (KatGs) are found not only in archaea and bacteria but also in lower eukaryotes. Structural studies and preliminary biochemical data of the secreted KatG from the rice pathogen Magnaporthe grisea (MagKatG2) suggested both similar and novel features when compared to those of the prokaryotic counterparts studied so far. In this work, we demonstrate the role of the autocatalytically formed redox-active Trp140-Tyr273-Met299 adduct of MagKatG2 in (i) the maintenance of the active site architecture, (ii) the catalysis of hydrogen peroxide dismutation, and (iii) the protein stability by comparing wild-type MagKatG2 with the single mutants Trp140Phe, Tyr273Phe, and Met299Ala. The impact of disruption of the covalent bonds between the adduct residues on the spectral signatures and heme cavity architecture was small. By contrast, loss of its integrity converts bifunctional MagKatG2 to a monofunctional peroxidase of significantly reduced thermal stability. It increases the accessibility of ligands due to the increased flexibility of the KatG-typical large loop 1 (LL1), which contributes to the substrate access channel and anchors at the adduct Tyr. We discuss these data with respect to those known from prokaryotic KatGs and in addition present a high-resolution structure of an oxoiron compound of MagKatG2.
Eukaryotic Catalase-Peroxidase: The Role of the Trp-Tyr-Met Adduct in Protein Stability, Substrate Accessibility, and Catalysis of Hydrogen Peroxide Dismutation.,Gasselhuber B, Carpena X, Graf MM, Pirker KF, Nicolussi A, Sundermann A, Hofbauer S, Zamocky M, Furtmuller PG, Jakopitsch C, Oostenbrink C, Fita I, Obinger C Biochemistry. 2015 Aug 25. PMID:26290940[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tanabe S, Ishii-Minami N, Saitoh K, Otake Y, Kaku H, Shibuya N, Nishizawa Y, Minami E. The role of catalase-peroxidase secreted by Magnaporthe oryzae during early infection of rice cells. Mol Plant Microbe Interact. 2011 Feb;24(2):163-71. doi: 10.1094/MPMI-07-10-0175. PMID:21043575 doi:10.1094/MPMI-07-10-0175
- ↑ Zamocky M, Droghetti E, Bellei M, Gasselhuber B, Pabst M, Furtmuller PG, Battistuzzi G, Smulevich G, Obinger C. Eukaryotic extracellular catalase-peroxidase from Magnaporthe grisea - Biophysical/chemical characterization of the first representative from a novel phytopathogenic KatG group. Biochimie. 2012 Mar;94(3):673-83. doi: 10.1016/j.biochi.2011.09.020. Epub 2011, Sep 29. PMID:21971530 doi:10.1016/j.biochi.2011.09.020
- ↑ Gasselhuber B, Carpena X, Graf MM, Pirker KF, Nicolussi A, Sundermann A, Hofbauer S, Zamocky M, Furtmuller PG, Jakopitsch C, Oostenbrink C, Fita I, Obinger C. Eukaryotic Catalase-Peroxidase: The Role of the Trp-Tyr-Met Adduct in Protein Stability, Substrate Accessibility, and Catalysis of Hydrogen Peroxide Dismutation. Biochemistry. 2015 Aug 25. PMID:26290940 doi:http://dx.doi.org/10.1021/acs.biochem.5b00831
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