View source for 7tmo


==V1 complex lacking subunit C from Saccharomyces cerevisiae, State 1==
<StructureSection load='7tmo' size='340' side='right'caption='[[7tmo]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7tmo]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TMO 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]] 3.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=7tmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tmo OCA], [https://pdbe.org/7tmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tmo RCSB], [https://www.ebi.ac.uk/pdbsum/7tmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tmo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VATE_YEAST VATE_YEAST] Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Vacuolar-type ATPases (V-ATPases) are rotary enzymes that acidify intracellular compartments in eukaryotic cells. These multi-subunit complexes consist of a cytoplasmic V(1) region that hydrolyzes ATP and a membrane-embedded V(O) region that transports protons. V-ATPase activity is regulated by reversible dissociation of the two regions, with the isolated V(1) and V(O) complexes becoming autoinhibited on disassembly and subunit C subsequently detaching from V(1). In yeast, assembly of the V(1) and V(O) regions is mediated by the regulator of the ATPase of vacuoles and endosomes (RAVE) complex through an unknown mechanism. We used cryogenic-electron microscopy of yeast V-ATPase to determine structures of the intact enzyme, the dissociated but complete V(1) complex and the V(1) complex lacking subunit C. On separation, V(1) undergoes a dramatic conformational rearrangement, with its rotational state becoming incompatible for reassembly with V(O). Loss of subunit C allows V(1) to match the rotational state of V(O), suggesting how RAVE could reassemble V(1) and V(O) by recruiting subunit C.

Coordinated conformational changes in the V(1) complex during V-ATPase reversible dissociation.,Vasanthakumar T, Keon KA, Bueler SA, Jaskolka MC, Rubinstein JL Nat Struct Mol Biol. 2022 May;29(5):430-439. doi: 10.1038/s41594-022-00757-z. , Epub 2022 Apr 25. PMID:35469063<ref>PMID:35469063</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7tmo" style="background-color:#fffaf0;"></div>

==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Bueler SA]]
[[Category: Jaskolka MC]]
[[Category: Keon KA]]
[[Category: Rubinstein JL]]
[[Category: Vasanthakumar T]]