7AHL

ALPHA-HEMOLYSIN FROM STAPHYLOCOCCUS AUREUS

7AHL の概要

• エントリーDOI: 10.2210/pdb7ahl/pdb
• 分子名称: ALPHA-HEMOLYSIN (2 entities in total)
• 機能のキーワード: hemolysin, transmembrane pore, cytolytic protein
• 由来する生物種: Staphylococcus aureus
• 細胞内の位置: Secreted: P09616
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 233030.00

構造登録者

Song, L.,Hobaugh, M.,Shustak, C.,Cheley, S.,Bayley, H.,Gouaux, J.E. (登録日: 1996-12-02, 公開日: 1998-01-14, 最終更新日: 2024-03-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.89 Å)