The projection structure of perfringolysin O (Clostridium perfringens theta-toxin).
The cytolysin Perfringolysin O was applied to lipid layers and the obtained ring-shaped oligomers analyzed by electron microscopy and image processing. The final result shows the periodic repeat of 2.4 nm along the outer rim of the ring. The asymmetric protein unit, corresponding to one monomer, spans the ring from the convex to the concave surface. It shows a clear protein peak close to the outer radius and less density in the middle of the oligomer. The number of monomers in the average ring is 50, and the inner radius of the aggregate is approximately 15 nm.
Olofsson
A
A
Center for Structural Biochemistry, Karolinska Institutet, NOVUM, Huddinge, Sweden.
Hebert
H
H
Thelestam
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M
D001427:Bacterial Toxins / Q000737:chemistry* / Q000378:metabolism; D001792:Blood Platelets / Q000737:chemistry; D003016:Clostridium perfringens; D006460:Hemolysin Proteins; D006801:Humans; D046911:Macromolecular Substances; D008563:Membrane Lipids / Q000378:metabolism; D008854:Microscopy, Electron
D001427:Bacterial Toxins; D006460:Hemolysin Proteins; D046911:Macromolecular Substances; D008563:Membrane Lipids; C020452:Clostridium perfringens theta-toxin