3AM2

Clostridium perfringens enterotoxin

Summary for 3AM2

• Entry DOI: 10.2210/pdb3am2/pdb
• Descriptor: Heat-labile enterotoxin B chain, UNKNOWN ATOM OR ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: pore forming toxins, toxin
• Biological source: Clostridium perfringens
• Total number of polymer chains: 1
• Total formula weight: 36658.64

Authors

Kitadokoro, K.,Nishimura, K.,Kamitani, S.,Kimura, J.,Fukui, A.,Abe, H.,Horiguchi, Y. (deposition date: 2010-08-12, release date: 2011-04-13, Last modification date: 2023-11-01)

Primary citation

Kitadokoro, K.,Nishimura, K.,Kamitani, S.,Fukui-Miyazaki, A.,Toshima, H.,Abe, H.,Kamata, Y.,Sugita-Konishi, Y.,Yamamoto, S.,Karatani, H.,Horiguchi, Y.
Crystal Structure of Clostridium perfringens Enterotoxin Displays Features of {beta}-Pore-forming Toxins
J.Biol.Chem., 286:19549-19555, 2011

PubMed 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 Laetiporus sulfureus hemolytic pore-forming lectin. The module is mainly made up of β-strands, two of which span its entire length. Domain II and domain III have three short β-strands each, by which they are distinguished. In addition, domain II has an α-helix lying on the β-strands. The sequence of amino acids composing the α-helix and preceding β-strand demonstrates an alternating pattern of hydrophobic residues that is characteristic of transmembrane domains forming β-barrel-made pores. These structural features imply that CPE is a β-pore-forming toxin. We also hypothesize that the transmembrane domain is inserted into the membrane upon the buckling of the two long β-strands spanning the module, a mechanism analogous to that of the cholesterol-dependent cytolysins.

PubMed: 21489981
DOI: 10.1074/jbc.M111.228478

Experimental method

X-RAY DIFFRACTION (2.51 Å)