TY - JOUR
T1 - Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
AU - Song, L.
AU - Hobaugh, M. R.
AU - Shustak, C.
AU - Cheley, S.
AU - Bayley, H.
AU - Gouaux, J. E.
PY - 1996/12/13
Y1 - 1996/12/13
N2 - 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.
AB - 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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U2 - 10.1126/science.274.5294.1859
DO - 10.1126/science.274.5294.1859
M3 - Article
C2 - 8943190
AN - SCOPUS:0030447720
SN - 0036-8075
VL - 274
SP - 1859
EP - 1866
JO - Science
JF - Science
IS - 5294
ER -