4cdb

Crystal structure of listeriolysin O

spinqualitylabelsall models 4cdb, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4cdb is a 1 chain structure with sequence from Listeria monocytogenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.15Å Ligands: ACT, NA, TAM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H3GD84_LISM4 A cholesterol-dependent toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol is required for binding to host membranes, membrane insertion and pore formation; cholesterol binding is mediated by a Thr-Leu pair in the C-terminus. Can be reversibly inactivated by oxidation.[RuleBase:RU364025] Publication Abstract from PubMed 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. Crystal structure of listeriolysin O reveals molecular details of oligomerization and pore formation.,Koster S, van Pee K, Hudel M, Leustik M, Rhinow D, Kuhlbrandt W, Chakraborty T, Yildiz O Nat Commun. 2014 Apr 22;5:3690. doi: 10.1038/ncomms4690. PMID:24751541 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytolysin 3D structures

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