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  • Open Access

Structure and function of C-terminal catalytic region of Pasteurella multocida toxin

  • 1Email author,
  • 2,
  • 2,
  • 2,
  • 2 and
  • 2
BMC Proceedings20082 (Suppl 1) :P32

https://doi.org/10.1186/1753-6561-2-s1-p32

  • Published:

Keywords

  • Disulfide
  • Disulfide Bond
  • Virulence Factor
  • Papain
  • Clostridium Difficile

Pasteurella multocida toxin (PMT) is one of the virulence factors responsible for 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 a Trojan horse structure, composed of three domains arranged in feet, body and head subunits with each linker loops, which were designated C1, C2, and C3 domains from the N- to C-terminus, respectively.

The C1 domain showing marked similarity in steric structure to the N-terminal domain of Clostridium difficile toxin B, was found to lead the toxin molecule to the plasma membrane. 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 indicate that PMT is an enzyme toxin carrying the cysteine protease-like catalytic triad dependent on the redox state, and functions oncytoplasmic face of the plasma membrane of target cells.

Authors’ Affiliations

(1)
Kyoto Institute of Technology, Matsugasakigosyokaidou-cho, Sakyo-ku, Kyoto Kyoto 606-8585, Japan
(2)
Research Institute for Microbial Diseases, Osaka University, Yamada-oka 3-1, Suita Osaka 565-0871, Japan

Copyright

© Kitadokoro et al; licensee BioMed Central Ltd. 2008

This article is published under license to BioMed Central Ltd.

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