3UT2

Crystal Structure of Fungal MagKatG2

3UT2 の概要

• エントリーDOI: 10.2210/pdb3ut2/pdb
• 分子名称: Catalase-peroxidase 2, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: catalase-peroxidase, katg, fungal, heme enzyme, oxidoreductase
• 由来する生物種: Magnaporthe oryzae 70-15 (Rice blast fungus)
• 細胞内の位置: Secreted : A4QUT2
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 168217.35

構造登録者

Zamocky, M.,Garcia-Fernandez, M.Q.,Gasselhuber, B.,Jakopitsch, C.,Furtmuller, P.G.,Loewen, P.C.,Fita, I.,Obinger, C.,Carpena, X. (登録日: 2011-11-24, 公開日: 2012-07-25, 最終更新日: 2023-12-06)

主引用文献

Zamocky, M.,Garcia-Fernandez, Q.,Gasselhuber, B.,Jakopitsch, C.,Furtmuller, P.G.,Loewen, P.C.,Fita, I.,Obinger, C.,Carpena, X.
High Conformational Stability of Secreted Eukaryotic Catalase-peroxidases: ANSWERS FROM FIRST CRYSTAL STRUCTURE AND UNFOLDING STUDIES.
J.Biol.Chem., 287:32254-32262, 2012

PubMed Abstract: Catalase-peroxidases (KatGs) are bifunctional heme enzymes widely spread in archaea, bacteria, and lower eukaryotes. Here we present the first crystal structure (1.55 Å 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 (+)Met-Tyr-Trp adduct (where the Trp is further modified by 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 cross-link the two subunits. Differential scanning calorimetry and temperature- and urea-mediated unfolding followed by UV-visible, 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 when compared with 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.

PubMed: 22822072
DOI: 10.1074/jbc.M112.384271

実験手法

X-RAY DIFFRACTION (1.549 Å)