2JH7
Crystal structure of Toxoplasma gondii micronemal protein 1 bound to 6'-sialyl-N-acetyllactosamine
Summary for 2JH7
| Entry DOI | 10.2210/pdb2jh7/pdb |
| Related | 2BVB 2JH1 2JHD |
| Descriptor | MICRONEMAL PROTEIN 1, N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose, ACETATE ION, ... (6 entities in total) |
| Functional Keywords | cell adhesion, mic1, microneme, mar domain, cell invasion |
| Biological source | TOXOPLASMA GONDII |
| Total number of polymer chains | 1 |
| Total formula weight | 28760.09 |
| Authors | Blumenschein, T.M.A.,Friedrich, N.,Childs, R.A.,Saouros, S.,Carpenter, E.P.,Campanero-Rhodes, M.A.,Simpson, P.,Koutroukides, T.,Blackman, M.J.,Feizi, T.,Soldati-Favre, D.,Matthews, S. (deposition date: 2007-02-20, release date: 2007-05-22, Last modification date: 2024-11-13) |
| Primary citation | Blumenschein, T.M.A.,Friedrich, N.,Childs, R.A.,Saouros, S.,Carpenter, E.P.,Campanero-Rhodes, M.A.,Simpson, P.,Chai, W.,Koutroukides, T.,Blackman, M.J.,Feizi, T.,Soldati-Favre, D.,Matthews, S. Atomic Resolution Insight Into Host Cell Recognition by Toxoplasma Gondii. Embo J., 26:2808-, 2007 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. Micronemal proteins (MICs) are released onto the parasite surface just before invasion of host cells and play important roles in host cell recognition, attachment and penetration. Here, we report the atomic structure for a key MIC, TgMIC1, and reveal a novel cell-binding motif called the microneme adhesive repeat (MAR). Using glycoarray analyses, we identified a novel interaction with sialylated oligosaccharides that resolves several prevailing misconceptions concerning TgMIC1. Structural studies of various complexes between TgMIC1 and sialylated oligosaccharides provide high-resolution insights into the recognition of sialylated oligosaccharides by a parasite surface protein. We observe that MAR domains exist in tandem repeats, which provide a highly specialized structure for glycan discrimination. Our work uncovers new features of parasite-receptor interactions at the early stages of host cell invasion, which will assist the design of new therapeutic strategies. PubMed: 17491595DOI: 10.1038/SJ.EMBOJ.7601704 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.07 Å) |
Structure validation
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