8FW5
Chimeric HsGATOR1-SpGtr-SpLam complex
Summary for 8FW5
| Entry DOI | 10.2210/pdb8fw5/pdb |
| EMDB information | 29497 |
| Descriptor | GATOR complex protein DEPDC5, GUANOSINE-5'-DIPHOSPHATE, ALUMINUM FLUORIDE, ... (12 entities in total) |
| Functional Keywords | mtor complex 1 (mtorc1), rag gtpase, gtr gtpase, lamtor, gator1, nutrient sensing, signaling protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 9 |
| Total formula weight | 451146.47 |
| Authors | Tettoni, S.D.,Egri, S.B.,Doxsey, D.D.,Ouch, C.,Chang, J.,Song, K.,Xu, C.,Shen, K. (deposition date: 2023-01-20, release date: 2023-07-26, Last modification date: 2023-09-20) |
| Primary citation | Tettoni, S.D.,Egri, S.B.,Doxsey, D.D.,Veinotte, K.,Ouch, C.,Chang, J.Y.,Song, K.,Xu, C.,Shen, K. Structure of the Schizosaccharomyces pombe Gtr-Lam complex reveals evolutionary divergence of mTORC1-dependent amino acid sensing. Structure, 31:1065-1076.e5, 2023 Cited by PubMed Abstract: mTORC1 is a protein kinase complex that controls cellular growth in response to nutrient availability. Amino acid signals are transmitted toward mTORC1 via the Rag/Gtr GTPases and their upstream regulators. An important regulator is LAMTOR, which localizes Rag/Gtr on the lysosomal/vacuole membrane. In human cells, LAMTOR consists of five subunits, but in yeast, only three or four. Currently, it is not known how variation of the subunit stoichiometry may affect its structural organization and biochemical properties. Here, we report a 3.1 Å-resolution structural model of the Gtr-Lam complex in Schizosaccharomyces pombe. We found that SpGtr shares conserved architecture as HsRag, but the intersubunit communication that coordinates nucleotide loading on the two subunits differs. In contrast, SpLam contains distinctive structural features, but its GTP-specific GEF activity toward SpGtr is evolutionarily conserved. Our results revealed unique evolutionary paths of the protein components of the mTORC1 pathway. PubMed: 37453417DOI: 10.1016/j.str.2023.06.012 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.08 Å) |
Structure validation
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