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Science 13 December 1996:
Vol. 274. no. 5294, pp. 1859 - 1865
DOI: 10.1126/science.274.5294.1859
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Research Articles

Structure of Staphylococcal alpha -Hemolysin, a Heptameric Transmembrane Pore

Langzhou Song, * Michael R. Hobaugh, * Christopher Shustak, Stephen Cheley, Hagan Bayley, J. Eric Gouaux dagger

The structure of the Staphylococcus aureus alpha -hemolysin pore has been determined to 1.9 Å resolution. Contained within the mushroom-shaped homo-oligomeric heptamer is a solvent-filled channel, 100 Å in length, that runs along the sevenfold axis and ranges from 14 Å to 46 Å 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 Å long. The interior of the beta  barrel is primarily hydrophilic, and the exterior has a hydrophobic belt 28 Å 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.

L. 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. C. Shustak, S. Cheley, and H. Bayley are with the Worcester Foundation for Biomedical Research, 222 Maple Avenue, Shrewsbury MA 01545, USA.
*   These authors made equal contributions to this work.

dagger    Present address: Department of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168 Street, New York, NY 10032, USA.

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