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The projection structure of Perfringolysin O (Clostridium perfringensθ-toxin)

Authors :
Monica Thelestam
Anders Olofsson
Hans Hebert
Source :
FEBS Letters. 319:125-127
Publication Year :
1993
Publisher :
Wiley, 1993.

Abstract

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.

Details

ISSN :
00145793
Volume :
319
Database :
OpenAIRE
Journal :
FEBS Letters
Accession number :
edsair.doi.dedup.....8c16f63016f2f36ef7b23d995b78f226
Full Text :
https://doi.org/10.1016/0014-5793(93)80050-5