5ouo

Structure of TgPLP1 APCbeta domain

spinqualitylabelsall models 5ouo, resolution 1.11Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ouo is a 1 chain structure with sequence from Toxoplasma gondii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.11Å Ligands: CL, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function V5BCL0_TOXGV Publication Abstract from PubMed Toxoplasma and Plasmodium are the parasitic agents of toxoplasmosis and malaria, respectively, and use perforin-like proteins (PLPs) to invade host organisms and complete their life cycles. The Toxoplasma gondii PLP1 (TgPLP1) is required for efficient exit from parasitophorous vacuoles in which proliferation occurs. We report structures of the membrane attack complex/perforin (MACPF) and Apicomplexan PLP C-terminal beta-pleated sheet (APCbeta) domains of TgPLP1. The MACPF domain forms hexameric assemblies, with ring and helix geometries, and the APCbeta domain has a novel beta-prism fold joined to the MACPF domain by a short linker. Molecular dynamics simulations suggest that the helical MACPF oligomer preserves a biologically important interface, whereas the APCbeta domain binds preferentially through a hydrophobic loop to membrane phosphatidylethanolamine, enhanced by the additional presence of inositol phosphate lipids. This mode of membrane binding is supported by site-directed mutagenesis data from a liposome-based assay. Together, these structural and biophysical findings provide insights into the molecular mechanism of membrane targeting by TgPLP1. Structures of monomeric and oligomeric forms of the Toxoplasma gondii perforin-like protein 1.,Ni T, Williams SI, Rezelj S, Anderluh G, Harlos K, Stansfeld PJ, Gilbert RJC Sci Adv. 2018 Mar 21;4(3):eaaq0762. doi: 10.1126/sciadv.aaq0762. eCollection 2018, Mar. PMID:29750191 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytolysin 3D structures

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