7U8O7U8O の概要
| エントリーDOI | 10.2210/pdb7u8o/pdb |
| EMDBエントリー | 26385 |
| 分子名称 | V-type proton ATPase catalytic subunit A, TLDc protein mEAK-7, V-type proton ATPase subunit a, ... (18 entities in total) |
| 機能のキーワード | proton translocation, complex, tldc, membrane protein |
| 由来する生物種 | Sus scrofa (pig) 詳細 |
| タンパク質・核酸の鎖数 | 36 |
| 化学式量合計 | 1214220.73 |
| 構造登録者 | |
| 主引用文献 | Tan, Y.Z.,Abbas, Y.M.,Wu, J.Z.,Wu, D.,Keon, K.A.,Hesketh, G.G.,Bueler, S.A.,Gingras, A.C.,Robinson, C.V.,Grinstein, S.,Rubinstein, J.L. CryoEM of endogenous mammalian V-ATPase interacting with the TLDc protein mEAK-7. Life Sci Alliance, 5:-, 2022 Cited by PubMed Abstract: V-ATPases are rotary proton pumps that serve as signaling hubs with numerous protein binding partners. CryoEM with exhaustive focused classification allowed detection of endogenous proteins associated with porcine kidney V-ATPase. An extra C subunit was found in ∼3% of complexes, whereas ∼1.6% of complexes bound mEAK-7, a protein with proposed roles in dauer formation in nematodes and mTOR signaling in mammals. High-resolution cryoEM of porcine kidney V-ATPase with recombinant mEAK-7 showed that mEAK-7's TLDc domain interacts with V-ATPase's stator, whereas its C-terminal α helix binds V-ATPase's rotor. This crosslink would be expected to inhibit rotary catalysis. However, unlike the yeast TLDc protein Oxr1p, exogenous mEAK-7 does not inhibit V-ATPase and mEAK-7 overexpression in cells does not alter lysosomal or phagosomal pH. Instead, cryoEM suggests that the mEAK-7:V-ATPase interaction is disrupted by ATP-induced rotation of the rotor. Comparison of Oxr1p and mEAK-7 binding explains this difference. These results show that V-ATPase binding by TLDc domain proteins can lead to effects ranging from strong inhibition to formation of labile interactions that are sensitive to the enzyme's activity. PubMed: 35794005DOI: 10.26508/lsa.202201527 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.5 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード
をダウンロード
