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RESEARCH PRODUCT
Structural characterization of the α-hemolysin monomer fromStaphylococcus aureus
Christian MeestersNadja HellmannHeinz DeckerAntje Bracksubject
LysisMolecular modelLeukocidinHemolysinBiochemistrychemistry.chemical_compoundCrystallographyMolecular dynamicsMonomerProtein structureMembranechemistryStructural BiologyMolecular Biologydescription
α-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 α-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 α-hemolysin, for example inherent flexibility, along with definite differences in comparison to the structures used as templates. Proteins 2009. © 2008 Wiley-Liss, Inc.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2008-09-17 | Proteins: Structure, Function, and Bioinformatics |