9BRD

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

This is a non-PDB format compatible entry.

Summary for 9BRD

• Entry DOI: 10.2210/pdb9brd/pdb
• EMDB information: 44353
• Descriptor: H(+)-transporting two-sector ATPase, V-type proton ATPase subunit H, Synaptophysin, ... (27 entities in total)
• Functional Keywords: vesicle, synaptic, membrane, proton transport
• Biological source: Legionella pneumophila subsp. pneumophila str. Philadelphia 1; More
• Total number of polymer chains: 36
• Total formula weight: 1310916.24

Authors

Coupland, C.E.,Rubinstein, J.L. (deposition date: 2024-05-11, release date: 2024-06-26, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.5 Å)