1QOY
E.coli Hemolysin E (HlyE, ClyA, SheA)
1QOY の概要
| エントリーDOI | 10.2210/pdb1qoy/pdb |
| 分子名称 | HEMOLYSIN E, SULFATE ION (3 entities in total) |
| 機能のキーワード | toxin, membrane pore former, cytolysin, hemolysin, pores |
| 由来する生物種 | ESCHERICHIA COLI |
| 細胞内の位置 | Secreted: P77335 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 35101.77 |
| 構造登録者 | Wallace, A.J.,Stillman, T.J.,Atkins, A.,Jamieson, S.J.,Bullough, P.A.,Green, J.,Artymiuk, P.J. (登録日: 1999-11-25, 公開日: 2000-01-23, 最終更新日: 2024-05-08) |
| 主引用文献 | Wallace, A.J.,Stillman, T.J.,Atkins, A.,Jamieson, S.J.,Bullough, P.A.,Green, J.,Artymiuk, P.J. E. Coli Hemolysin E (Hlye, Clya, Shea): X-Ray Crystal Structure of the Toxin and Observation of Membrane Pores by Electron Microscopy Cell(Cambridge,Mass.), 100:265-, 2000 Cited by PubMed Abstract: Hemolysin E (HlyE) is a novel pore-forming toxin of Escherichia coli, Salmonella typhi, and Shigella flexneri. Here we report the X-ray crystal structure of the water-soluble form of E. coli HlyE at 2.0 A resolution and the visualization of the lipid-associated form of the toxin in projection at low resolution by electron microscopy. The crystal structure reveals HlyE to be the first member of a new family of toxin structures, consisting of an elaborated helical bundle some 100 A long. The electron micrographs show how HlyE oligomerizes in the presence of lipid to form transmembrane pores. Taken together, the data from these two structural techniques allow us to propose a simple model for the structure of the pore and for membrane interaction. PubMed: 10660049DOI: 10.1016/S0092-8674(00)81564-0 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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