Structure of a quinohemoprotein amine dehydrogenase with an uncommon redox cofactor and highly unusual crosslinking

DOI Web Site 被引用文献20件
  • Saumen Datta
    Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110; Department of Structural Molecular Biology, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan; and Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan
  • Youichi Mori
    Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110; Department of Structural Molecular Biology, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan; and Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan
  • Kazuyoshi Takagi
    Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110; Department of Structural Molecular Biology, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan; and Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan
  • Katsunori Kawaguchi
    Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110; Department of Structural Molecular Biology, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan; and Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan
  • Zhi-Wei Chen
    Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110; Department of Structural Molecular Biology, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan; and Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan
  • Toshihide Okajima
    Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110; Department of Structural Molecular Biology, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan; and Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan
  • Shun'ichi Kuroda
    Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110; Department of Structural Molecular Biology, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan; and Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan
  • Tokuji Ikeda
    Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110; Department of Structural Molecular Biology, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan; and Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan
  • Kenji Kano
    Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110; Department of Structural Molecular Biology, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan; and Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan
  • Katsuyuki Tanizawa
    Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110; Department of Structural Molecular Biology, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan; and Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan
  • F. Scott Mathews
    Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110; Department of Structural Molecular Biology, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan; and Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan

抄録

<jats:p> The crystal structure of the heterotrimeric quinohemoprotein amine dehydrogenase from <jats:italic>Paracoccus denitrificans</jats:italic> has been determined at 2.05-Å resolution. Within an 82-residue subunit is contained an unusual redox cofactor, cysteine tryptophylquinone (CTQ), consisting of an orthoquinone-modified tryptophan side chain covalently linked to a nearby cysteine side chain. The subunit is surrounded on three sides by a 489-residue, four-domain subunit that includes a diheme cytochrome <jats:italic>c</jats:italic> . Both subunits sit on the surface of a third subunit, a 337-residue seven-bladed β-propeller that forms part of the enzyme active site. The small catalytic subunit is internally crosslinked by three highly unusual covalent cysteine to aspartic or glutamic acid thioether linkages in addition to the cofactor crossbridge. The catalytic function of the enzyme as well as the biosynthesis of the unusual catalytic subunit is discussed. </jats:p>

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