4CDB
Crystal structure of listeriolysin O
4CDB の概要
| エントリーDOI | 10.2210/pdb4cdb/pdb |
| 分子名称 | LISTERIOLYSIN O, ACETATE ION, SODIUM ION, ... (5 entities in total) |
| 機能のキーワード | toxin, cholesterol dependent cytolysin, membrane perforation, hemolysis |
| 由来する生物種 | LISTERIA MONOCYTOGENES |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 54991.71 |
| 構造登録者 | |
| 主引用文献 | Koester, S.,Pee, K.V.,Hudel, M.,Leustik, M.,Rhinow, D.,Kuehlbrandt, W.,Chakraborty, T.,Yildiz, O. Crystal Structure of Listeriolysin O Reveals Molecular Details of Oligomerization and Pore Formation Nat.Commun., 5:3690-, 2014 Cited by PubMed Abstract: Listeriolysin O (LLO) is an essential virulence factor of Listeria monocytogenes that causes listeriosis. Listeria monocytogenes owes its ability to live within cells to the pH- and temperature-dependent pore-forming activity of LLO, which is unique among cholesterol-dependent cytolysins. LLO enables the bacteria to cross the phagosomal membrane and is also involved in activation of cellular processes, including the modulation of gene expression or intracellular Ca(2+) oscillations. Neither the pore-forming mechanism nor the mechanisms triggering the signalling processes in the host cell are known in detail. Here, we report the crystal structure of LLO, in which we identified regions important for oligomerization and pore formation. Mutants were characterized by determining their haemolytic and Ca(2+) uptake activity. We analysed the pore formation of LLO and its variants on erythrocyte ghosts by electron microscopy and show that pore formation requires precise interface interactions during toxin oligomerization on the membrane. PubMed: 24751541DOI: 10.1038/NCOMMS4690 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.15 Å) |
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