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Crystal structure of Clostridium perfringens enterotoxin displays features of beta-pore-forming toxins.


ABSTRACT: Clostridium perfringens enterotoxin (CPE) is a cause of food poisoning and is considered a pore-forming toxin, which damages target cells by disrupting the selective permeability of the plasma membrane. However, the pore-forming mechanism and the structural characteristics of the pores are not well documented. Here, we present the structure of CPE determined by x-ray crystallography at 2.0 Å. The overall structure of CPE displays an elongated shape, composed of three distinct domains, I, II, and III. Domain I corresponds to the region that was formerly referred to as C-CPE, which is responsible for binding to the specific receptor claudin. Domains II and III comprise a characteristic module, which resembles those of ?-pore-forming toxins such as aerolysin, C. perfringens ?-toxin, and Laetiporus sulfureus hemolytic pore-forming lectin. The module is mainly made up of ?-strands, two of which span its entire length. Domain II and domain III have three short ?-strands each, by which they are distinguished. In addition, domain II has an ?-helix lying on the ?-strands. The sequence of amino acids composing the ?-helix and preceding ?-strand demonstrates an alternating pattern of hydrophobic residues that is characteristic of transmembrane domains forming ?-barrel-made pores. These structural features imply that CPE is a ?-pore-forming toxin. We also hypothesize that the transmembrane domain is inserted into the membrane upon the buckling of the two long ?-strands spanning the module, a mechanism analogous to that of the cholesterol-dependent cytolysins.

SUBMITTER: Kitadokoro K 

PROVIDER: S-EPMC3103334 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature

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Crystal structure of Clostridium perfringens enterotoxin displays features of beta-pore-forming toxins.

Kitadokoro Kengo K   Nishimura Kousuke K   Kamitani Shigeki S   Fukui-Miyazaki Aya A   Toshima Hirono H   Abe Hiroyuki H   Kamata Yoichi Y   Sugita-Konishi Yoshiko Y   Yamamoto Shigeki S   Karatani Hajime H   Horiguchi Yasuhiko Y  

The Journal of biological chemistry 20110412 22


Clostridium perfringens enterotoxin (CPE) is a cause of food poisoning and is considered a pore-forming toxin, which damages target cells by disrupting the selective permeability of the plasma membrane. However, the pore-forming mechanism and the structural characteristics of the pores are not well documented. Here, we present the structure of CPE determined by x-ray crystallography at 2.0 Å. The overall structure of CPE displays an elongated shape, composed of three distinct domains, I, II, and  ...[more]

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