Structural and functional analogy between pneumolysin and proaerolysin

R Sowdhamini, T J Mitchell, P W Andrew, P J Morgan

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


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 languageEnglish
Pages (from-to)207-15
Number of pages9
JournalProtein Engineering
Issue number3
Publication statusPublished - Mar 1997


  • 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


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