Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore.
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,...
| Main Authors: | , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
1996
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| _version_ | 1826274594129969152 |
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| author | Song, L Hobaugh, MR Shustak, C Cheley, S Bayley, J Gouaux, J |
| author_facet | Song, L Hobaugh, MR Shustak, C Cheley, S Bayley, J Gouaux, J |
| author_sort | Song, L |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T22:45:49Z |
| format | Journal article |
| id | oxford-uuid:5d2220c8-2720-4736-b78a-c18f1aea83bc |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T22:45:49Z |
| publishDate | 1996 |
| record_format | dspace |
| spelling | oxford-uuid:5d2220c8-2720-4736-b78a-c18f1aea83bc2022-03-26T17:32:30ZStructure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:5d2220c8-2720-4736-b78a-c18f1aea83bcEnglishSymplectic Elements at Oxford1996Song, LHobaugh, MRShustak, CCheley, SBayley, JGouaux, JThe 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. |
| spellingShingle | Song, L Hobaugh, MR Shustak, C Cheley, S Bayley, J Gouaux, J Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. |
| title | Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. |
| title_full | Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. |
| title_fullStr | Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. |
| title_full_unstemmed | Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. |
| title_short | Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. |
| title_sort | structure of staphylococcal alpha hemolysin a heptameric transmembrane pore |
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