7AHL

ALPHA-HEMOLYSIN FROM STAPHYLOCOCCUS AUREUS

Summary for 7AHL

• Entry DOI: 10.2210/pdb7ahl/pdb
• Descriptor: ALPHA-HEMOLYSIN (2 entities in total)
• Functional Keywords: hemolysin, transmembrane pore, cytolytic protein
• Biological source: Staphylococcus aureus
• Cellular location: Secreted: P09616
• Total number of polymer chains: 7
• Total formula weight: 233030.00

Authors

Song, L.,Hobaugh, M.,Shustak, C.,Cheley, S.,Bayley, H.,Gouaux, J.E. (deposition date: 1996-12-02, release date: 1998-01-14, Last modification date: 2024-03-06)

Primary citation

Song, L.,Hobaugh, M.R.,Shustak, C.,Cheley, S.,Bayley, H.,Gouaux, J.E.
Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore.
Science, 274:1859-1866, 1996

PubMed Abstract: 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.

PubMed: 8943190
DOI: 10.1126/science.274.5294.1859

Experimental method

X-RAY DIFFRACTION (1.89 Å)