4CDB
Crystal structure of listeriolysin O
Summary for 4CDB
| Entry DOI | 10.2210/pdb4cdb/pdb |
| Descriptor | LISTERIOLYSIN O, ACETATE ION, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | toxin, cholesterol dependent cytolysin, membrane perforation, hemolysis |
| Biological source | LISTERIA MONOCYTOGENES |
| Total number of polymer chains | 1 |
| Total formula weight | 54991.71 |
| Authors | Koester, S.,Yildiz, O. (deposition date: 2013-10-30, release date: 2014-04-23, Last modification date: 2023-12-20) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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