7tmr
From Proteopedia
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==V-ATPase from Saccharomyces cerevisiae, State 1== | ==V-ATPase from Saccharomyces cerevisiae, State 1== | ||
| - | <StructureSection load='7tmr' size='340' side='right'caption='[[7tmr]]' scene=''> | + | <StructureSection load='7tmr' size='340' side='right'caption='[[7tmr]], [[Resolution|resolution]] 3.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TMR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7tmr]] is a 18 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=7TMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TMR FirstGlance]. <br> |
| - | </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=7tmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tmr OCA], [https://pdbe.org/7tmr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tmr RCSB], [https://www.ebi.ac.uk/pdbsum/7tmr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tmr ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</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></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=7tmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tmr OCA], [https://pdbe.org/7tmr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tmr RCSB], [https://www.ebi.ac.uk/pdbsum/7tmr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tmr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/VATA_YEAST VATA_YEAST] Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase (vacuolar ATPase) is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. It is an electrogenic proton pump that generates a proton motive force of 180 mV, inside positive and acidic, in the vacuolar membrane vesicles. It may participate in maintenance of cytoplasmic Ca(2+) homeostasis. This is a catalytic subunit.<ref>PMID:1534148</ref> PI-SceI is an endonuclease that can cleave at a site present in a VMA1 allele that lacks the derived endonuclease segment of the open reading frame; cleavage at this site only occurs during meiosis and initiates "homing", a genetic event that converts a VMA1 allele lacking VDE into one that contains it.<ref>PMID:1534148</ref> | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7tmr" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[ATPase 3D structures|ATPase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Bueler SA]] | [[Category: Bueler SA]] | ||
[[Category: Jaskolka MC]] | [[Category: Jaskolka MC]] | ||
Current revision
V-ATPase from Saccharomyces cerevisiae, State 1
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