9B8Q

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

Summary for 9B8Q

• Entry DOI: 10.2210/pdb9b8q/pdb
• Related: 9B8O 9B8P 9BRB 9BRC 9BRD
• EMDB information: 44350 44351 44352 44353 44354 44355
• Descriptor: V-type proton ATPase subunit C 1, V-type proton ATPase subunit E 1, V-type proton ATPase subunit G, ... (5 entities in total)
• Functional Keywords: complex, synaptic, native, proton transport
• Biological source: Rattus norvegicus (Norway rat); More
• Total number of polymer chains: 9
• Total formula weight: 315898.63

Authors

Coupland, C.E.,Rubinstein, J.L. (deposition date: 2024-03-31, release date: 2024-06-26, Last modification date: 2024-07-24)

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 loss of V 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 (3.8 Å)