6m0s: Difference between revisions
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==3.6A Yeast Vo state3 prime== | |||
<StructureSection load='6m0s' size='340' side='right'caption='[[6m0s]], [[Resolution|resolution]] 3.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6m0s]] is a 15 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=6M0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M0S 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]] 3.6Å</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=6m0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m0s OCA], [https://pdbe.org/6m0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m0s RCSB], [https://www.ebi.ac.uk/pdbsum/6m0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m0s ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/VPP1_YEAST VPP1_YEAST] Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:1491220, PubMed:8798414, PubMed:11278748). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:1491220, PubMed:11278748). Is present only in vacuolar V-ATPase complexes; enzymes containing this subunit have a 4-fold higher ratio of proton transport to ATP hydrolysis than complexes containing the Golgi/endosomal isoform and undergo reversible dissociation of V1 and V0 in response to glucose depletion (PubMed:8798414, PubMed:11278748).<ref>PMID:11278748</ref> <ref>PMID:1491220</ref> <ref>PMID:8798414</ref> | |||
==See Also== | |||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
== References == | |||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae S288C]] | ||
[[Category: | [[Category: Chipot C]] | ||
[[Category: Shekhar | [[Category: Chiu W]] | ||
[[Category: | [[Category: Pintilie G]] | ||
[[Category: Roh SH]] | |||
[[Category: SIngharoy A]] | |||
[[Category: Shekhar M]] | |||
[[Category: Wilkens S]] | |||
Latest revision as of 13:48, 27 March 2024
3.6A Yeast Vo state3 prime3.6A Yeast Vo state3 prime
Structural highlights
FunctionVPP1_YEAST Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:1491220, PubMed:8798414, PubMed:11278748). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:1491220, PubMed:11278748). Is present only in vacuolar V-ATPase complexes; enzymes containing this subunit have a 4-fold higher ratio of proton transport to ATP hydrolysis than complexes containing the Golgi/endosomal isoform and undergo reversible dissociation of V1 and V0 in response to glucose depletion (PubMed:8798414, PubMed:11278748).[1] [2] [3] See AlsoReferences
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