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Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore

Langzhou SongL. Song, M. R. Hobaugh, and J. E. Gouaux are in the Department of Biochemistry and Molecular Biology, The University of Chicago, 920 East 58 Street, Chicago, IL 60637, USAMichael R. HobaughL. Song, M. R. Hobaugh, and J. E. Gouaux are in the Department of Biochemistry and Molecular Biology, The University of Chicago, 920 East 58 Street, Chicago, IL 60637, USAC. ShustakC. Shustak, S. Cheley, and H. Bayley are with the Worcester Foundation for Biomedical Research, 222 Maple Avenue, Shrewsbury MA 01545, USAStephen CheleyC. Shustak, S. Cheley, and H. Bayley are with the Worcester Foundation for Biomedical Research, 222 Maple Avenue, Shrewsbury MA 01545, USAHagan BayleyC. Shustak, S. Cheley, and H. Bayley are with the Worcester Foundation for Biomedical Research, 222 Maple Avenue, Shrewsbury MA 01545, USAJ. Eric GouauxL. Song, M. R. Hobaugh, and J. E. Gouaux are in the Department of Biochemistry and Molecular Biology, The University of Chicago, 920 East 58 Street, Chicago, IL 60637, USA

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Annotatsiya

The structure of the Staphylococcus aureus alpha-hemolysin pore has been determined to 1.9 A resolution. Contained within the mushroom-shaped homo-oligomeric heptamer is a solvent-filled channel, 100 A in length, that runs along the sevenfold axis and ranges from 14 A to 46 A in diameter. The lytic, transmembrane domain comprises the lower half of a 14-strand antiparallel beta barrel, to which each protomer contributes two beta strands, each 65 A long. The interior of the beta barrel is primarily hydrophilic, and the exterior has a hydrophobic belt 28 A wide. The structure proves the heptameric subunit stoichiometry of the alpha-hemolysin oligomer, shows that a glycine-rich and solvent-exposed region of a water-soluble protein can self-assemble to form a transmembrane pore of defined structure, and provides insight into the principles of membrane interaction and transport activity of beta barrel pore-forming toxins.

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Identifikatorlar

DOI: 10.1126/science.274.5294.1859

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