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| | <StructureSection load='5oup' size='340' side='right'caption='[[5oup]], [[Resolution|resolution]] 2.03Å' scene=''> | | <StructureSection load='5oup' size='340' side='right'caption='[[5oup]], [[Resolution|resolution]] 2.03Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5oup]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxgo Toxgo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OUP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OUP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5oup]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OUP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.03Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PLP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5811 TOXGO])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5oup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oup OCA], [http://pdbe.org/5oup PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oup RCSB], [http://www.ebi.ac.uk/pdbsum/5oup PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oup ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5oup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oup OCA], [https://pdbe.org/5oup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oup RCSB], [https://www.ebi.ac.uk/pdbsum/5oup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oup ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/V5BCL0_TOXGV V5BCL0_TOXGV] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5oup" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5oup" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Cytolysin 3D structures|Cytolysin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Toxgo]] | + | [[Category: Toxoplasma gondii]] |
| - | [[Category: Gilbert, R J.C]] | + | [[Category: Gilbert RJC]] |
| - | [[Category: Ni, T]] | + | [[Category: Ni T]] |
| - | [[Category: Cell egress]]
| + | |
| - | [[Category: Lipid binding protein]]
| + | |
| - | [[Category: Macpf domain]]
| + | |
| - | [[Category: Toxoplasma]]
| + | |
| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ni T, Williams SI, Rezelj S, Anderluh G, Harlos K, Stansfeld PJ, Gilbert RJC. Structures of monomeric and oligomeric forms of the Toxoplasma gondii perforin-like protein 1. Sci Adv. 2018 Mar 21;4(3):eaaq0762. doi: 10.1126/sciadv.aaq0762. eCollection 2018, Mar. PMID:29750191 doi:http://dx.doi.org/10.1126/sciadv.aaq0762
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