9B8P
Synaptic Vesicle V-ATPase with synaptophysin and SidK, State 3, V1
This is a non-PDB format compatible entry.
Summary for 9B8P
| Entry DOI | 10.2210/pdb9b8p/pdb |
| Related | 9B8O 9B8Q 9BRB 9BRC 9BRD |
| EMDB information | 44350 44351 44352 44353 44354 44355 |
| Descriptor | H(+)-transporting two-sector ATPase, V-type proton ATPase subunit B, brain isoform, ATPase H+-transporting V1 subunit D, ... (8 entities in total) |
| Functional Keywords | mmebrane, synaptic, complex, proton transport |
| Biological source | Legionella pneumophila subsp. pneumophila str. Philadelphia 1 More |
| Total number of polymer chains | 17 |
| Total formula weight | 742550.18 |
| Authors | Coupland, E.M.,Rubinstein, J.L. (deposition date: 2024-03-31, release date: 2024-07-03, 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 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 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: 38900912DOI: 10.1126/science.adp5577 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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