Structural and functional analogy between pneumolysin and proaerolysin

Research output: Contribution to journalArticlepeer-review

Authors

Colleges, School and Institutes

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.

Details

Original languageEnglish
Pages (from-to)207-15
Number of pages9
JournalProtein Engineering
Volume10
Issue number3
Publication statusPublished - 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