9BRC の概要
| エントリーDOI | 10.2210/pdb9brc/pdb |
| EMDBエントリー | 44354 |
| 分子名称 | H(+)-transporting two-sector ATPase, V-type proton ATPase subunit H, Synaptophysin, ... (18 entities in total) |
| 機能のキーワード | synaptic, vesicle, membrane, proton transport |
| 由来する生物種 | Legionella pneumophila subsp. pneumophila 詳細 |
| タンパク質・核酸の鎖数 | 36 |
| 化学式量合計 | 1283886.31 |
| 構造登録者 | |
| 主引用文献 | Coupland, C.E.,Karimi, R.,Bueler, S.A.,Liang, Y.,Courbon, G.M.,Di Trani, J.M.,Wong, C.J.,Saghian, R.,Youn, J.Y.,Wang, L.Y.,Rubinstein, J.L. High-resolution electron cryomicroscopy of V-ATPase in native synaptic vesicles. Science, 385:168-174, 2024 Cited by PubMed Abstract: Intercellular communication in the nervous system occurs through the release of neurotransmitters into the synaptic cleft between neurons. In the presynaptic neuron, the proton pumping vesicular- or vacuolar-type ATPase (V-ATPase) powers neurotransmitter loading into synaptic vesicles (SVs), with the V complex dissociating from the membrane region of the enzyme before exocytosis. We isolated SVs from rat brain using SidK, a V-ATPase-binding bacterial effector protein. Single particle electron cryomicroscopy allowed high-resolution structure determination of V-ATPase within the native SV membrane. In the structure, regularly spaced cholesterol molecules decorate the enzyme's rotor and the abundant SV protein synaptophysin binds the complex stoichiometrically. ATP hydrolysis during vesicle loading results in loss of V from the SV membrane, suggesting that loading is sufficient to induce dissociation of the enzyme. PubMed: 38900912DOI: 10.1126/science.adp5577 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.9 Å) |
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