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==Crystal Structure of the Heterotrimeric EGChead Peripheral Stalk Complex of the Yeast Vacuolar ATPase - second conformation== | |||
<StructureSection load='4efa' size='340' side='right'caption='[[4efa]], [[Resolution|resolution]] 2.82Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4efa]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EFA FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8163Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4efa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4efa OCA], [https://pdbe.org/4efa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4efa RCSB], [https://www.ebi.ac.uk/pdbsum/4efa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4efa ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/VATC_YEAST VATC_YEAST] Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C acts as a flexible stator that holds together the catalytic and the membrane sectors of the enzyme. Reversibly leaves the enzyme after glucose depletion, causing the catalytic subcomplex V1 to detach from the V0 section. Binds ATP and is likely to have a specific function in the catalytic activity of the catalytic sector. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.<ref>PMID:10781598</ref> | |||
== | ==See Also== | ||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae S288C]] | |||
[[Category: | [[Category: Berry EA]] | ||
[[Category: | [[Category: Huang LS]] | ||
[[Category: | [[Category: Oot RA]] | ||
[[Category: | [[Category: Wilkens S]] | ||
[[Category: | |||
[[Category: |
Latest revision as of 18:00, 14 March 2024
Crystal Structure of the Heterotrimeric EGChead Peripheral Stalk Complex of the Yeast Vacuolar ATPase - second conformationCrystal Structure of the Heterotrimeric EGChead Peripheral Stalk Complex of the Yeast Vacuolar ATPase - second conformation
Structural highlights
FunctionVATC_YEAST Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C acts as a flexible stator that holds together the catalytic and the membrane sectors of the enzyme. Reversibly leaves the enzyme after glucose depletion, causing the catalytic subcomplex V1 to detach from the V0 section. Binds ATP and is likely to have a specific function in the catalytic activity of the catalytic sector. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.[1] See AlsoReferences
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