Abstract
Pneumolysin is a membrane-damaging toxin produced by Streptococcus pneumoniae. In order to understand fully the mode of action of this toxin, it is necessary to have an appreciation of the size, self-association behaviour and solution conformation of pneumolysin. A combination of analytical ultracentrifugation methodologies has shown that pneumolysin lacks self-association behaviour in solution and has provided a weight-average M(r) (M omega) of 52,000 +/- 2000, which was in agreement with that derived from the amino acid sequence. By determining a sedimentation coefficient (S20,w0) of 3.35 +/- 0.10 S, it was possible to suggest a model for the gross solution conformation of pneumolysin monomers. Spectroscopic methods provide additional secondary and tertiary structure information.
Original language | English |
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Pages (from-to) | 671-4 |
Number of pages | 4 |
Journal | Biochemical Journal |
Volume | 296 ( Pt 3) |
Publication status | Published - 15 Dec 1993 |
Keywords
- Amino Acids
- Bacterial Proteins
- Cell Membrane
- Circular Dichroism
- Cytotoxins
- Protein Structure, Secondary
- Solutions
- Spectrometry, Fluorescence
- Spectrophotometry, Ultraviolet
- Streptococcus pneumoniae
- Streptolysins
- Ultracentrifugation