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 β-pore-forming toxins such as aerolysin, C. perfringens ε-toxin, and Laeti

SUBMITTER: Kitadokoro K 

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

REPOSITORIES: biostudies-literature