View source for 9b8q


==Synaptic Vesicle V-ATPase with synaptophysin and SidK, State 3, peripheral stalks==
<StructureSection load='9b8q' size='340' side='right'caption='[[9b8q]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9b8q]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9B8Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9B8Q FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9b8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9b8q OCA], [https://pdbe.org/9b8q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9b8q RCSB], [https://www.ebi.ac.uk/pdbsum/9b8q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9b8q ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VATC1_RAT VATC1_RAT] Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (By similarity).
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== Publication Abstract from PubMed ==
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(1) 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(1) from the SV membrane, suggesting that loading is sufficient to induce dissociation of the enzyme.

High-resolution electron cryomicroscopy of V-ATPase in native synaptic vesicles.,Coupland CE, Karimi R, Bueler SA, Liang Y, Courbon GM, Di Trani JM, Wong CJ, Saghian R, Youn JY, Wang LY, Rubinstein JL Science. 2024 Jun 20:eadp5577. doi: 10.1126/science.adp5577. PMID:38900912<ref>PMID:38900912</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9b8q" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Coupland CE]]
[[Category: Rubinstein JL]]