Structural characterization of the alpha-hemolysin monomer from Staphylococcus aureus.
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.
Meesters
Christian
C
Institute of Molecular Biophysics, University of Mainz, Mainz, Germany. meesters@uni-mainz.de
Brack
Antje
A
Hellmann
Nadja
N
Decker
Heinz
H
D001427:Bacterial Toxins / Q000737:chemistry*; D006460:Hemolysin Proteins / Q000737:chemistry*; D007956:Leukocidins / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D053838:Scattering, Small Angle; D013211:Staphylococcus aureus / Q000737:chemistry*; D014961:X-Ray Diffraction
D001427:Bacterial Toxins; D006460:Hemolysin Proteins; D007956:Leukocidins; C021091:staphylococcal alpha-toxin