Structure and Function of C-terminal Catalytic Region of Pasteurella Multocida Toxin

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  • KITADOKORO Kengo
    Graduate School of Science and Technology, Department of Biomolecular Engineering, Kyoto Institute of Technology
  • KAMITANI Shigeki
    Department of Molecular Bacteriology, Research Institute for Microbial Diseases, Osaka University
  • HORIGUCHI Yasuhiko
    Department of Molecular Bacteriology, Research Institute for Microbial Diseases, Osaka University

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  • 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
  • Pasteurella multocida ユライ ノ サイキン ドクソ ノ サイボウナイ キノウ リョウイキ ノ コウゾウ ト キノウ カイセキ

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Abstract

Pasteurella multocida toxin (PMT) is one of virulence factors responsible for the pathogenesis in some Pasteurellosis. 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.

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