Pasteurella multocida 由来の細菌毒素の細胞内機能領域の構造と機能解析 Structure and Function of C-terminal Catalytic Region of Pasteurella Multocida Toxin

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著者

    • 北所 健悟 KITADOKORO Kengo
    • 京都工芸繊維大学大学院工芸科学研究科生体分子工学部門 Graduate School of Science and Technology, Department of Biomolecular Engineering, Kyoto Institute of Technology
    • 神谷 重樹 KAMITANI Shigeki
    • 大阪大学微生物病研究所分子細菌学分野 Department of Molecular Bacteriology, Research Institute for Microbial Diseases, Osaka University
    • 堀口 安彦 HORIGUCHI Yasuhiko
    • 大阪大学微生物病研究所分子細菌学分野 Department of Molecular Bacteriology, Research Institute for Microbial Diseases, Osaka University

抄録

<I>Pasteurella multocida</I> toxin (PMT) is one of virulence factors responsible for the pathogenesis in some <I>Pasteurellosis</I>. We determined the crystal structure of the C-terminal region of PMT (C-PMT), which carries an intracellularly active moiety. The overall structure of C-PMT displays three different domains designated C1, C2 and C3. We found in the C3 domain the Cys-His-Asp catalytic triad that is organized only when the Cys is released from a disulfide bond. The steric alignment of the triad corresponded well to that of papain or other enzymes carrying the Cys-His-Asp triad. Our results demonstrate that PMT is an enzymatic toxin carrying the cysteine-protease like catalytic triad, which is organized only under reducing conditions.

収録刊行物

  • 日本結晶学会誌  

    日本結晶学会誌 50(3), 187-193, 2008-06-30 

    The Crystallographic Society of Japan

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各種コード

  • NII論文ID(NAID)
    10021085809
  • NII書誌ID(NCID)
    AN00188364
  • 本文言語コード
    JPN
  • 資料種別
    ART
  • ISSN
    03694585
  • NDL 記事登録ID
    9576814
  • NDL 雑誌分類
    ZM46(科学技術--地球科学--岩石・鉱物・鉱床)
  • NDL 請求記号
    Z15-138
  • データ提供元
    CJP書誌  NDL  J-STAGE 
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