Abstract
Pneumolysin and proaerolysin are bacterial toxins that form pores in host cells by oligomerization. We propose that they may have similar structures despite a poor sequence identity. The crystal structure of proaerolysin reveals a protein composed of four domains, arranged in the shape of an elongated comma. Electron microscopy of the pneumolysin monomer shows a similar arrangement of domains. The sequence of pneumolysin recognizes the template of proaerolysin from a library of protein folds. A three-dimensional model of pneumolysin has been constructed by the comparative approach using the structure of proaerolysin. This model, together with results on the activity of site-specific mutants and the positions of antigenic sites, has been used to propose functional roles of individual domains.
Original language | English |
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Pages (from-to) | 207-15 |
Number of pages | 9 |
Journal | Protein Engineering |
Volume | 10 |
Issue number | 3 |
Publication status | Published - Mar 1997 |
Keywords
- Amino Acid Sequence
- Bacterial Proteins
- Bacterial Toxins
- Crystallography, X-Ray
- Hemolysin Proteins
- Microscopy, Electron
- Models, Molecular
- Molecular Sequence Data
- Pore Forming Cytotoxic Proteins
- Protein Conformation
- Protein Folding
- Protein Structure, Secondary
- Sequence Alignment
- Software
- Streptolysins
- Structure-Activity Relationship