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The projection structure of Perfringolysin O (Clostridium perfringensθ-toxin)
- 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.
- Subjects :
- Blood Platelets
Clostridium perfringens
Macromolecular Substances
Bacterial Toxins
Biophysics
Ring (chemistry)
medicine.disease_cause
Cholesterol-dependent cytolysin
Biochemistry
Oligomer
law.invention
Hemolysin Proteins
Membrane Lipids
chemistry.chemical_compound
Image processing
Structural Biology
law
Genetics
medicine
Humans
Molecule
Molecular Biology
Quantitative Biology::Biomolecules
Cell Biology
Radius
Microscopy, Electron
Perfringolysin O, Electron microscopy
Crystallography
Monomer
chemistry
Electron microscope
Subjects
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