3ut2
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==Crystal Structure of Fungal MagKatG2== | |
| - | === | + | <StructureSection load='3ut2' size='340' side='right' caption='[[3ut2]], [[Resolution|resolution]] 1.55Å' scene=''> |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3ut2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Magnaporthe_oryzae_70-15 Magnaporthe oryzae 70-15]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UT2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UT2 FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> |
| + | <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> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">katG2, MagKatG2, MGG_09834 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=242507 Magnaporthe oryzae 70-15])</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=3ut2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ut2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ut2 RCSB], [http://www.ebi.ac.uk/pdbsum/3ut2 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == 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> | [[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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | CatalaseAperoxidases (KatGs) are bifunctional heme enzymes widely spread in archaea, bacteria and lower eukaryotes. Here we present the first crystal structure (1.55 A resolution) of an eukaryotic KatG, the extracellular or secreted enzyme from the phytopathogenic fungus Magnaporthe grisea. The heme cavity of the homodimeric enzyme is similar to prokaryotic KatGs including the unique distal (+)MetATyrATrp adduct (where the Trp is further modified by a peroxidation) and its associated mobile arginine. The structure also revealed several conspicuous peculiarities that are fully conserved in all secreted eukaryotic KatGs. Peculiarities include the wrapping at the dimer interface of the N-terminal elongations from the two subunits and cysteine residues that crosslink the two subunits. Differential scanning calorimetry, temperature- and urea-mediated unfolding followed by UVAVis, circular dichroism and fluorescence spectroscopy combined with site-directed mutagenesis demonstrated that secreted eukaryotic KatGs have a significantly higher conformational stability as well as a different unfolding pattern compared to intracellular eukaryotic and prokaryotic catalase-peroxidases. We discuss these properties with respect to the structure as well as the postulated roles of this metalloenzyme in host-pathogen interactions. | ||
| + | |||
| + | High conformational stability of secreted eukaryotic catalase-peroxidases -answers from first crystal structure and unfolding studies.,Zamocky M, Garcia-Fernandez Q, Gasselhuber B, Jakopitsch C, Furtmuller PG, Loewen PC, Fita I, Obinger C, Carpena X J Biol Chem. 2012 Jul 27. PMID:22822072<ref>PMID:22822072</ref> | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | ==See Also== |
| - | <references | + | *[[Catalase|Catalase]] |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Catalase peroxidase]] | [[Category: Catalase peroxidase]] | ||
[[Category: Magnaporthe oryzae 70-15]] | [[Category: Magnaporthe oryzae 70-15]] | ||
| - | [[Category: Carpena, X | + | [[Category: Carpena, X]] |
| - | [[Category: Fita, I | + | [[Category: Fita, I]] |
| - | [[Category: Furtmuller, P G | + | [[Category: Furtmuller, P G]] |
| - | [[Category: Garcia-Fernandez, M Q | + | [[Category: Garcia-Fernandez, M Q]] |
| - | [[Category: Gasselhuber, B | + | [[Category: Gasselhuber, B]] |
| - | [[Category: Jakopitsch, C | + | [[Category: Jakopitsch, C]] |
[[Category: Loewen, P C]] | [[Category: Loewen, P C]] | ||
| - | [[Category: Obinger, C | + | [[Category: Obinger, C]] |
| - | [[Category: Zamocky, M | + | [[Category: Zamocky, M]] |
[[Category: Catalase-peroxidase]] | [[Category: Catalase-peroxidase]] | ||
[[Category: Fungal]] | [[Category: Fungal]] | ||
Revision as of 18:49, 24 December 2014
Crystal Structure of Fungal MagKatG2
| |||||||||||
