3R7W
Crystal Structure of Gtr1p-Gtr2p complex
3R7W の概要
| エントリーDOI | 10.2210/pdb3r7w/pdb |
| 分子名称 | GTP-binding protein GTR1, GTP-binding protein GTR2, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (5 entities in total) |
| 機能のキーワード | rag gtpases, gtr1p, gtr2p, mtor, protein transport |
| 由来する生物種 | Saccharomyces cerevisiae (yeast) 詳細 |
| 細胞内の位置 | Vacuole membrane: Q00582 P53290 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 150394.65 |
| 構造登録者 | |
| 主引用文献 | Gong, R.,Li, L.,Liu, Y.,Wang, P.,Yang, H.,Wang, L.,Cheng, J.,Guan, K.L.,Xu, Y. Crystal structure of the Gtr1p-Gtr2p complex reveals new insights into the amino acid-induced TORC1 activation Genes Dev., 25:1668-1673, 2011 Cited by PubMed Abstract: The target of rapamycin (TOR) complex 1 (TORC1) is a central cell growth regulator in response to a wide array of signals. The Rag GTPases play an essential role in relaying amino acid signals to TORC1 activation through direct interaction with raptor and recruitment of the TORC1 complex to lysosomes. Here we present the crystal structure of the Gtr1p-Gtr2p complex, the Rag homologs from Saccharomyces cerevisiae, at 2.8 Å resolution. The heterodimeric GTPases reveal a pseudo-twofold symmetric organization. Structure-guided functional analyses of RagA-RagC, the human homologs of Gtr1p-Gtr2p, show that both G domains (N-terminal GTPase domains) and dimerization are important for raptor binding. In particular, the switch regions of the G domain in RagA are indispensible for interaction with raptor, and hence TORC1 activation. The dimerized C-terminal domains of RagA-RagC display a remarkable structural similarity to MP1/p14, which is in a complex with lysosome membrane protein p18, and directly interact with p18, therefore recruiting mTORC1 to the lysosome for activation by Rheb. Our results reveal a structural model for the mechanism of the Rag GTPases in TORC1 activation and amino acid signaling. PubMed: 21816923DOI: 10.1101/gad.16968011 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.773 Å) |
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