The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore
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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Keyburn, A. L., Boyce, J. D., Vaz, P., Bannam, T. L., Ford, M. E., Parker, D., Di Rubbo, A., Rood, J. I., & Moore, R. J. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.0040026 · Cited by 624
Metadata
- Authors
- Song, L., Hobaugh, M. R., Shustak, C., Cheley, S., Bayley, H., & Gouaux, J. E.
- Venue
- Science
- Published
- 1996-12-13
- Volume
- 274
- Issue
- 5294
- Pages
- 1859-1865
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2030683115
- Cited by
- 2,377
- References
- 41
- FWCI
- 50.38
- Type
- journal article
- Language
- en
- Open access
- closed
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- Song, L., Hobaugh, M. R., Shustak, C., Cheley, S., Bayley, H., & Gouaux, J. E. (1996). Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore. Science. https://doi.org/10.1126/science.274.5294.1859
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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