7U4T の概要
エントリーDOI | 10.2210/pdb7u4t/pdb |
関連するPDBエントリー | 6WM3 |
EMDBエントリー | 26334 |
分子名称 | V-type proton ATPase 116 kDa subunit a isoform 1, V-type proton ATPase 16 kDa proteolipid subunit, V-type proton ATPase subunit d 1, ... (20 entities in total) |
機能のキーワード | v-atpase, meak-7, membrane protein |
由来する生物種 | Legionella pneumophila 詳細 |
タンパク質・核酸の鎖数 | 36 |
化学式量合計 | 1302060.01 |
構造登録者 | |
主引用文献 | Wang, L.,Wu, D.,Robinson, C.V.,Fu, T.M. Identification of mEAK-7 as a human V-ATPase regulator via cryo-EM data mining. Proc.Natl.Acad.Sci.USA, 119:e2203742119-e2203742119, 2022 Cited by PubMed Abstract: Vacuolar-type adenosine triphosphatases (V-ATPases) not only function as rotary proton pumps in cellular organelles but also serve as signaling hubs. To identify the endogenous binding partners of V-ATPase, we collected a large dataset of human V-ATPases and did extensive classification and focused refinement of human V-ATPases. Unexpectedly, about 17% of particles in state 2 of human V-ATPases display additional density with an overall resolution of 3.3 Å. Structural analysis combined with artificial intelligence modeling enables us to identify this additional density as mEAK-7, a protein involved in mechanistic target of rapamycin (mTOR) signaling in mammals. Our structure shows that mEAK-7 interacts with subunits A, B, D, and E of V-ATPases in state 2. Thus, we propose that mEAK-7 may regulate V-ATPase function through binding to V-ATPases in state 2 as well as mediate mTOR signaling. PubMed: 35994636DOI: 10.1073/pnas.2203742119 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.6 Å) |
構造検証レポート
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