3am2

Clostridium perfringens enterotoxinClostridium perfringens enterotoxin

Structural highlights 3am2 is a 1 chain structure with sequence from Clostridium perfringens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.51Å Ligands: , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ELTB_CLOPF This enterotoxin is responsible for many cases of a mild type of food poisoning. Publication Abstract from PubMed 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 A. 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 beta-pore-forming toxins such as aerolysin, C. perfringens epsilon-toxin, and Laetiporus sulfureus hemolytic pore-forming lectin. The module is mainly made up of beta-strands, two of which span its entire length. Domain II and domain III have three short beta-strands each, by which they are distinguished. In addition, domain II has an alpha-helix lying on the beta-strands. The sequence of amino acids composing the alpha-helix and preceding beta-strand demonstrates an alternating pattern of hydrophobic residues that is characteristic of transmembrane domains forming beta-barrel-made pores. These structural features imply that CPE is a beta-pore-forming toxin. We also hypothesize that the transmembrane domain is inserted into the membrane upon the buckling of the two long beta-strands spanning the module, a mechanism analogous to that of the cholesterol-dependent cytolysins. Crystal Structure of Clostridium perfringens Enterotoxin Displays Features of {beta}-Pore-forming Toxins.,Kitadokoro K, Nishimura K, Kamitani S, Fukui-Miyazaki A, Toshima H, Abe H, Kamata Y, Sugita-Konishi Y, Yamamoto S, Karatani H, Horiguchi Y J Biol Chem. 2011 Jun 3;286(22):19549-55. Epub 2011 Apr 12. PMID:21489981 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 3am2, resolution 2.51Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image