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| - | {{Seed}} | |
| - | [[Image:2k2t.jpg|left|200px]] | |
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| - | <!-- | + | ==Epidermal growth Factor-like domain 2 from Toxoplasma gondii Microneme protein 6== |
| - | The line below this paragraph, containing "STRUCTURE_2k2t", creates the "Structure Box" on the page.
| + | <StructureSection load='2k2t' size='340' side='right'caption='[[2k2t]]' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[2k2t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K2T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K2T FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</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=2k2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2t OCA], [https://pdbe.org/2k2t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k2t RCSB], [https://www.ebi.ac.uk/pdbsum/2k2t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k2t ProSAT]</span></td></tr> |
| - | {{STRUCTURE_2k2t| PDB=2k2t | SCENE= }}
| + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/MIC6_TOXGO MIC6_TOXGO] Escorter protein required for import of MIC1 and MIC4 adhesins into the microneme.<ref>PMID:11157983</ref> <ref>PMID:16166092</ref> <ref>PMID:18818666</ref> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | The obligate intracellular parasite Toxoplasma gondii, a member of the phylum Apicomplexa that includes Plasmodium spp., is one of the most widespread parasites and the causative agent of toxoplasmosis. Adhesive complexes composed of microneme proteins (MICs) are secreted onto the parasite surface from intracellular stores and fulfil crucial roles in host-cell recognition, attachment and penetration. Here, we report the high-resolution solution structure of a complex between two crucial MICs, TgMIC6 and TgMIC1. Furthermore, we identify two analogous interaction sites within separate epidermal growth factor-like (EGF) domains of TgMIC6-EGF2 and EGF3-and confirm that both interactions are functional for the recognition of host cell receptor in the parasite, using immunofluorescence and invasion assays. The nature of this new mode of recognition of the EGF domain and its abundance in apicomplexan surface proteins suggest a more generalized means of constructing functional assemblies by using EGF domains with highly specific receptor-binding properties. |
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| - | ===Epidermal growth Factor-like domain 2 from Toxoplasma gondii Microneme protein 6===
| + | Structural insights into microneme protein assembly reveal a new mode of EGF domain recognition.,Sawmynaden K, Saouros S, Friedrich N, Marchant J, Simpson P, Bleijlevens B, Blackman MJ, Soldati-Favre D, Matthews S EMBO Rep. 2008 Nov;9(11):1149-55. Epub 2008 Sep 26. PMID:18818666<ref>PMID:18818666</ref> |
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| - | | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | <!--
| + | </div> |
| - | The line below this paragraph, {{ABSTRACT_PUBMED_18818666}}, adds the Publication Abstract to the page
| + | <div class="pdbe-citations 2k2t" style="background-color:#fffaf0;"></div> |
| - | (as it appears on PubMed at http://www.pubmed.gov), where 18818666 is the PubMed ID number.
| + | == References == |
| - | -->
| + | <references/> |
| - | {{ABSTRACT_PUBMED_18818666}}
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | ==About this Structure== | + | [[Category: Large Structures]] |
| - | 2K2T is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K2T OCA].
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| - | | + | |
| - | ==Reference== | + | |
| - | <ref group="xtra">PMID:18818666</ref><references group="xtra"/> | + | |
| | [[Category: Toxoplasma gondii]] | | [[Category: Toxoplasma gondii]] |
| - | [[Category: Marchant, J.]] | + | [[Category: Marchant J]] |
| - | [[Category: Matthews, S.]] | + | [[Category: Matthews S]] |
| - | [[Category: Saouros, S.]] | + | [[Category: Saouros S]] |
| - | [[Category: Sawmynaden, K.]] | + | [[Category: Sawmynaden K]] |
| - | [[Category: Simpson, P.]] | + | [[Category: Simpson P]] |
| - | [[Category: Apicomplexa]]
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| - | [[Category: Cell adhesion]]
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| - | [[Category: Cytoplasmic vesicle]]
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| - | [[Category: Egf]]
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| - | [[Category: Egf-like domain]]
| + | |
| - | [[Category: Membrane]]
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| - | [[Category: Mic6]]
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| - | [[Category: Protozoa]]
| + | |
| - | [[Category: Toxoplasma gondii]]
| + | |
| - | [[Category: Transmembrane]]
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| - | [[Category: Virulence]]
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 25 09:18:01 2009''
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| Structural highlights
Function
MIC6_TOXGO Escorter protein required for import of MIC1 and MIC4 adhesins into the microneme.[1] [2] [3]
Publication Abstract from PubMed
The obligate intracellular parasite Toxoplasma gondii, a member of the phylum Apicomplexa that includes Plasmodium spp., is one of the most widespread parasites and the causative agent of toxoplasmosis. Adhesive complexes composed of microneme proteins (MICs) are secreted onto the parasite surface from intracellular stores and fulfil crucial roles in host-cell recognition, attachment and penetration. Here, we report the high-resolution solution structure of a complex between two crucial MICs, TgMIC6 and TgMIC1. Furthermore, we identify two analogous interaction sites within separate epidermal growth factor-like (EGF) domains of TgMIC6-EGF2 and EGF3-and confirm that both interactions are functional for the recognition of host cell receptor in the parasite, using immunofluorescence and invasion assays. The nature of this new mode of recognition of the EGF domain and its abundance in apicomplexan surface proteins suggest a more generalized means of constructing functional assemblies by using EGF domains with highly specific receptor-binding properties.
Structural insights into microneme protein assembly reveal a new mode of EGF domain recognition.,Sawmynaden K, Saouros S, Friedrich N, Marchant J, Simpson P, Bleijlevens B, Blackman MJ, Soldati-Favre D, Matthews S EMBO Rep. 2008 Nov;9(11):1149-55. Epub 2008 Sep 26. PMID:18818666[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Reiss M, Viebig N, Brecht S, Fourmaux MN, Soete M, Di Cristina M, Dubremetz JF, Soldati D. Identification and characterization of an escorter for two secretory adhesins in Toxoplasma gondii. J Cell Biol. 2001 Feb 5;152(3):563-78. PMID:11157983
- ↑ Saouros S, Edwards-Jones B, Reiss M, Sawmynaden K, Cota E, Simpson P, Dowse TJ, Jakle U, Ramboarina S, Shivarattan T, Matthews S, Soldati-Favre D. A novel galectin-like domain from Toxoplasma gondii micronemal protein 1 assists the folding, assembly, and transport of a cell adhesion complex. J Biol Chem. 2005 Nov 18;280(46):38583-91. Epub 2005 Sep 15. PMID:16166092 doi:C500365200
- ↑ Sawmynaden K, Saouros S, Friedrich N, Marchant J, Simpson P, Bleijlevens B, Blackman MJ, Soldati-Favre D, Matthews S. Structural insights into microneme protein assembly reveal a new mode of EGF domain recognition. EMBO Rep. 2008 Nov;9(11):1149-55. Epub 2008 Sep 26. PMID:18818666 doi:10.1038/embor.2008.179
- ↑ Sawmynaden K, Saouros S, Friedrich N, Marchant J, Simpson P, Bleijlevens B, Blackman MJ, Soldati-Favre D, Matthews S. Structural insights into microneme protein assembly reveal a new mode of EGF domain recognition. EMBO Rep. 2008 Nov;9(11):1149-55. Epub 2008 Sep 26. PMID:18818666 doi:10.1038/embor.2008.179
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