2BVB
The C-terminal domain from Micronemal Protein 1 (MIC1) from Toxoplasma Gondii
Summary for 2BVB
| Entry DOI | 10.2210/pdb2bvb/pdb |
| NMR Information | BMRB: 6376 |
| Descriptor | MICRONEMAL PROTEIN 1 (1 entity in total) |
| Functional Keywords | mic1, microneme, invasion, adhesion |
| Biological source | TOXOPLASMA GONDII |
| Cellular location | Cytoplasmic vesicle, secretory vesicle, microneme: O00834 |
| Total number of polymer chains | 1 |
| Total formula weight | 14030.57 |
| Authors | Saouros, S.,Edwards-Jones, B.,Reiss, M.,Sawmynaden, K.,Cota, E.,Simpson, P.,Dowse, T.J.,Jakle, U.,Ramboarina, S.,Shivarattan, T.,Matthews, S.,Soldati-Favre, D. (deposition date: 2005-06-23, release date: 2005-10-12, Last modification date: 2024-11-06) |
| Primary citation | Saouros, S.,Edwards-Jones, B.,Reiss, M.,Sawmynaden, K.,Cota, E.,Simpson, P.,Dowse, T.J.,Jakle, U.,Ramboarina, S.,Shivarattan, T.,Matthews, S.,Soldati-Favre, D. A Novel Galectin-Like Domain from Toxoplasma Gondll Micronemal Protein 1 Assists the Folding, Assembly,and Transport of a Cell-Adhesion Complex. J.Biol.Chem., 280:38583-, 2005 Cited by PubMed Abstract: Immediately prior to invasion Toxoplasma gondii tachyzoites release a large number of micronemal proteins (TgMICs) that participate in host cell attachment and penetration. The TgMIC4-MIC1-MIC6 complex was the first to be identified in T. gondii and has been recently shown to be critical in invasion. This study establishes that the N-terminal thrombospondin type I repeat-like domains (TSR1-like) from TgMIC1 function as an independent adhesin as well as promoting association with TgMIC4. Using the newly solved three-dimensional structure of the C-terminal domain of TgMIC1 we have identified a novel Galectin-like fold that does not possess carbohydrate binding properties and redefines the architecture of TgMIC1. Instead, the TgMIC1 Galectin-like domain interacts and stabilizes TgMIC6, which provides the basis for a highly specific quality control mechanism for successful exit from the early secretory compartments and for subsequent trafficking of the complex to the micronemes. PubMed: 16166092DOI: 10.1074/JBC.C500365200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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