Abstract
The structure of the Staphylococcus aureus α-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 β barrel, to which each protomer contributes two β strands, each 65 Å long. The interior of the β barrel is primarily hydrophilic, and the exterior has a hydrophobic belt 28 Å wide. The structure proves the heptameric subunit stoichiometry of the α-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 β barrel pore-forming toxins.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 27, 2002, 5:37 a.m.) |
Deposited | 1 year ago (Aug. 7, 2024, 7:27 a.m.) |
Indexed | 14 hours, 58 minutes ago (Sept. 3, 2025, 6:58 a.m.) |
Issued | 28 years, 8 months ago (Dec. 13, 1996) |
Published | 28 years, 8 months ago (Dec. 13, 1996) |
Published Print | 28 years, 8 months ago (Dec. 13, 1996) |
@article{Song_1996, title={Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore}, volume={274}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.274.5294.1859}, DOI={10.1126/science.274.5294.1859}, number={5294}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Song, Langzhou and Hobaugh, Michael R. and Shustak, Christopher and Cheley, Stephen and Bayley, Hagan and Gouaux, J. Eric}, year={1996}, month=dec, pages={1859–1865} }