2K2T
Epidermal growth Factor-like domain 2 from Toxoplasma gondii Microneme protein 6
Summary for 2K2T
| Entry DOI | 10.2210/pdb2k2t/pdb |
| Related | 2K2S |
| Descriptor | Micronemal protein 6 (1 entity in total) |
| Functional Keywords | egf, mic6, toxoplasma gondii, apicomplexa, protozoa, cell adhesion, cytoplasmic vesicle, egf-like domain, membrane, transmembrane, virulence |
| Biological source | Toxoplasma gondii |
| Cellular location | Cytoplasmic vesicle, secretory vesicle, microneme membrane; Single-pass type I membrane protein: Q9XYH7 |
| Total number of polymer chains | 1 |
| Total formula weight | 6366.06 |
| Authors | Sawmynaden, K.,Saouros, S.,Marchant, J.,Simpson, P.,Matthews, S. (deposition date: 2008-04-11, release date: 2009-02-24, Last modification date: 2024-11-06) |
| Primary citation | Sawmynaden, K.,Saouros, S.,Friedrich, N.,Marchant, J.,Simpson, P.,Bleijlevens, B.,Blackman, M.J.,Soldati-Favre, D.,Matthews, S. Structural insights into microneme protein assembly reveal a new mode of EGF domain recognition. Embo Rep., 9:1149-1155, 2008 Cited by PubMed Abstract: 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. PubMed: 18818666DOI: 10.1038/embor.2008.179 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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