View source for 9brb


==Synaptic Vesicle V-ATPase with synaptophysin and SidK, State 1==
<StructureSection load='9brb' size='340' side='right'caption='[[9brb]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9brb]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila Legionella pneumophila subsp. pneumophila] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9BRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9BRB 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]] 3.6&#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=9brb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9brb OCA], [https://pdbe.org/9brb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9brb RCSB], [https://www.ebi.ac.uk/pdbsum/9brb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9brb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VATL_RAT VATL_RAT] Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. 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 9brb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Legionella pneumophila subsp. pneumophila]]
[[Category: Rattus norvegicus]]
[[Category: Coupland CE]]
[[Category: Rubinstein JL]]