6pe4: Difference between revisions

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==Yeast Vo motor in complex with 1 VopQ molecule==
==Yeast Vo motor in complex with 1 VopQ molecule==
<StructureSection load='6pe4' size='340' side='right'caption='[[6pe4]]' scene=''>
<StructureSection load='6pe4' size='340' side='right'caption='[[6pe4]], [[Resolution|resolution]] 3.10&Aring;' 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=6PE4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6PE4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6pe4]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C] and [https://en.wikipedia.org/wiki/Vibrio_parahaemolyticus Vibrio parahaemolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PE4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PE4 FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6pe4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pe4 OCA], [http://pdbe.org/6pe4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pe4 RCSB], [http://www.ebi.ac.uk/pdbsum/6pe4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pe4 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]] 3.1&#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=6pe4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pe4 OCA], [https://pdbe.org/6pe4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pe4 RCSB], [https://www.ebi.ac.uk/pdbsum/6pe4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pe4 ProSAT]</span></td></tr>
</table>
</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 ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Vibrio parahaemolyticus]]
[[Category: Li Y]]
[[Category: Li Y]]
[[Category: Orth K]]
[[Category: Orth K]]
[[Category: Peng W]]
[[Category: Peng W]]
[[Category: Tomchick DR]]
[[Category: Tomchick DR]]

Latest revision as of 12:26, 20 March 2024

Yeast Vo motor in complex with 1 VopQ moleculeYeast Vo motor in complex with 1 VopQ molecule

Structural highlights

6pe4 is a 16 chain structure with sequence from Saccharomyces cerevisiae S288C and Vibrio parahaemolyticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.1Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1] [2] [3]

See Also

References

  1. ↑ Kawasaki-Nishi S, Nishi T, Forgac M. Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-subunit differ in coupling efficiency and in vivo dissociation. J Biol Chem. 2001 May 25;276(21):17941-8. Epub 2001 Mar 2. PMID:11278748 doi:http://dx.doi.org/10.1074/jbc.M010790200
  2. ↑ Manolson MF, Proteau D, Jones EW. Evidence for a conserved 95-120 kDa subunit associated with and essential for activity of V-ATPases. J Exp Biol. 1992 Nov;172:105-12. PMID:1491220
  3. ↑ Leng XH, Manolson MF, Liu Q, Forgac M. Site-directed mutagenesis of the 100-kDa subunit (Vph1p) of the yeast vacuolar (H+)-ATPase. J Biol Chem. 1996 Sep 13;271(37):22487-93. PMID:8798414

6pe4, resolution 3.10Å

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