2N2Y
Solution structure of the meiosis-expressed gene 1 (Meig1)
Summary for 2N2Y
| Entry DOI | 10.2210/pdb2n2y/pdb |
| NMR Information | BMRB: 25627 |
| Descriptor | Meiosis-expressed gene 1 protein (1 entity in total) |
| Functional Keywords | cell cycle |
| Biological source | Mus musculus (mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 11256.78 |
| Authors | Williams Jr., D.C.,Walavalkar, N.M.,Buchwald, W.A. (deposition date: 2015-05-16, release date: 2016-01-20, Last modification date: 2024-05-15) |
| Primary citation | Li, W.,Walavalkar, N.M.,Buchwald, W.A.,Teves, M.E.,Zhang, L.,Liu, H.,Bilinovich, S.,Peterson, D.L.,Strauss Iii, J.F.,Williams, D.C.,Zhang, Z. Dissecting the structural basis of MEIG1 interaction with PACRG. Sci Rep, 6:18278-18278, 2016 Cited by PubMed Abstract: The product of the meiosis-expressed gene 1 (MEIG1) is found in the cell bodies of spermatocytes and recruited to the manchette, a structure unique to elongating spermatids, by Parkin co-regulated gene (PACRG). This complex is essential for targeting cargo to the manchette during sperm flagellum assembly. Here we show that MEIG1 adopts a unique fold that provides a large surface for interacting with other proteins. We mutated 12 exposed and conserved amino acids and show that four of these mutations (W50A, K57E, F66A, Y68A) dramatically reduce binding to PACRG. These four amino acids form a contiguous hydrophobic patch on one end of the protein. Furthermore, each of these four mutations diminishes the ability of MEIG1 to stabilize PACRG when expressed in bacteria. Together these studies establish the unique structure and key interaction surface of MEIG1 and provide a framework to explore how MEIG1 recruits proteins to build the sperm tail. PubMed: 26726850DOI: 10.1038/srep18278 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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