3ut2

Crystal Structure of Fungal MagKatG2

spinqualitylabelsall models 3ut2, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ut2 is a 2 chain structure with sequence from Pyricularia oryzae 70-15. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.549Å Ligands: HEM, TOX Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function KATG2_PYRO7 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.[HAMAP-Rule:MF_03108] 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Catalase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA