4A5V
Solution structure ensemble of the two N-terminal apple domains (residues 58-231) of Toxoplasma gondii microneme protein 4
Summary for 4A5V
| Entry DOI | 10.2210/pdb4a5v/pdb |
| NMR Information | BMRB: 18039 |
| Descriptor | MICRONEMAL PROTEIN 4 (1 entity in total) |
| Functional Keywords | adhesion |
| Biological source | TOXOPLASMA GONDII |
| Cellular location | Cytoplasmic vesicle, secretory vesicle, microneme: Q9XZH7 |
| Total number of polymer chains | 1 |
| Total formula weight | 17243.07 |
| Authors | Marchant, J.,Cowper, B.,Liu, Y.,Lai, L.,Pinzan, C.,Marq, J.B.,Friedrich, N.,Sawmynaden, K.,Chai, W.,Childs, R.A.,Saouros, S.,Simpson, P.,Barreira, M.C.R.,Feizi, T.,Soldati-Favre, D.,Matthews, S. (deposition date: 2011-10-28, release date: 2012-04-04, Last modification date: 2023-06-14) |
| Primary citation | Marchant, J.,Cowper, B.,Liu, Y.,Lai, L.,Pinzan, C.,Marq, J.B.,Friedrich, N.,Sawmynaden, K.,Liew, L.,Chai, W.,Childs, R.A.,Saouros, S.,Simpson, P.,Roque Barreira, M.C.,Feizi, T.,Soldati-Favre, D.,Matthews, S. Galactose Recognition by the Apicomplexan Parasite Toxoplasma Gondii. J.Biol.Chem., 287:16720-, 2012 Cited by PubMed Abstract: Toxosplasma gondii is the model parasite of the phylum Apicomplexa, which contains numerous obligate intracellular parasites of medical and veterinary importance, including Eimeria, Sarcocystis, Cryptosporidium, Cyclospora, and Plasmodium species. Members of this phylum actively enter host cells by a multistep process with the help of microneme protein (MIC) complexes that play important roles in motility, host cell attachment, moving junction formation, and invasion. T. gondii (Tg)MIC1-4-6 complex is the most extensively investigated microneme complex, which contributes to host cell recognition and attachment via the action of TgMIC1, a sialic acid-binding adhesin. Here, we report the structure of TgMIC4 and reveal its carbohydrate-binding specificity to a variety of galactose-containing carbohydrate ligands. The lectin is composed of six apple domains in which the fifth domain displays a potent galactose-binding activity, and which is cleaved from the complex during parasite invasion. We propose that galactose recognition by TgMIC4 may compromise host protection from galectin-mediated activation of the host immune system. PubMed: 22399295DOI: 10.1074/JBC.M111.325928 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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