9B8P

Synaptic Vesicle V-ATPase with synaptophysin and SidK, State 3, V1

これはPDB形式変換不可エントリーです。

9B8P の概要

• エントリーDOI: 10.2210/pdb9b8p/pdb
• 関連するPDBエントリー: 9B8O 9B8Q 9BRB 9BRC 9BRD
• EMDBエントリー: 44350 44351 44352 44353 44354 44355
• 分子名称: H(+)-transporting two-sector ATPase, V-type proton ATPase subunit B, brain isoform, ATPase H+-transporting V1 subunit D, ... (8 entities in total)
• 機能のキーワード: mmebrane, synaptic, complex, proton transport
• 由来する生物種: Legionella pneumophila subsp. pneumophila str. Philadelphia 1; 詳細
• タンパク質・核酸の鎖数: 17
• 化学式量合計: 742550.18

構造登録者

Coupland, E.M.,Rubinstein, J.L. (登録日: 2024-03-31, 公開日: 2024-07-03, 最終更新日: 2024-07-24)

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

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 a loss of the V region of V-ATPase from the SV membrane, suggesting that loading is sufficient to induce dissociation of the enzyme.

PubMed: 38900912
DOI: 10.1126/science.adp5577

実験手法

ELECTRON MICROSCOPY (3.2 Å)