Structural characterization of the alpha-hemolysin monomer from Staphylococcus aureus

Proteins. 2009 Apr;75(1):118-26. doi: 10.1002/prot.22227.


Alpha-hemolysin from Staphylococcus aureus is secreted as a water-soluble monomer and assembles on membranes to oligomerize into a homo-heptameric, water-filled pore. These pores lead to lysis and cell death. Although the structure of the heptameric pore is solved by means of X-ray crystallography, structures of intermediate states-from the soluble monomer to all potential "pre-pore" structures-are yet unknown. Here, we propose a model of the monomeric alpha-hemolysin in solution based on molecular modeling, verified by small angle X-ray scattering data. This structure reveals details of the monomeric conformation of the alpha-hemolysin, for example inherent flexibility, along with definite differences in comparison to the structures used as templates.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Toxins / chemistry*
  • Hemolysin Proteins / chemistry*
  • Leukocidins / chemistry
  • Models, Molecular
  • Protein Conformation
  • Protein Multimerization
  • Protein Structure, Secondary
  • Scattering, Small Angle
  • Staphylococcus aureus / chemistry*
  • X-Ray Diffraction


  • Bacterial Toxins
  • Hemolysin Proteins
  • Leukocidins
  • staphylococcal alpha-toxin