6o7x

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==Saccharomyces cerevisiae V-ATPase Stv1-V1VO State 3==
==Saccharomyces cerevisiae V-ATPase Stv1-V1VO State 3==
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<StructureSection load='6o7x' size='340' side='right'caption='[[6o7x]], [[Resolution|resolution]] 8.70&Aring;' scene=''>
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<SX load='6o7x' size='340' side='right' viewer='molstar' caption='[[6o7x]], [[Resolution|resolution]] 8.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6o7x]] is a 31 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae], [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_(strain_atcc_204508_/_s288c) Saccharomyces cerevisiae (strain atcc 204508 / s288c)] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_(strain_rm11-1a) Saccharomyces cerevisiae (strain rm11-1a)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O7X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6O7X FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6o7x]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae], [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_RM11-1a Saccharomyces cerevisiae RM11-1a] and [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=6O7X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O7X FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6o7t|6o7t]], [[6o7u|6o7u]], [[6o7v|6o7v]], [[6o7w|6o7w]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8.7&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6o7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o7x OCA], [http://pdbe.org/6o7x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o7x RCSB], [http://www.ebi.ac.uk/pdbsum/6o7x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o7x ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6o7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o7x OCA], [https://pdbe.org/6o7x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o7x RCSB], [https://www.ebi.ac.uk/pdbsum/6o7x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o7x ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/VATO_YEAST VATO_YEAST]] Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. [[http://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. [[http://www.uniprot.org/uniprot/VATD_YEAST VATD_YEAST]] Subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system. [[http://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> [[http://www.uniprot.org/uniprot/VATL1_YEAST VATL1_YEAST]] Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-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. [[http://www.uniprot.org/uniprot/VATG_YEAST VATG_YEAST]] Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. [[http://www.uniprot.org/uniprot/VATF_YEAST VATF_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. [[http://www.uniprot.org/uniprot/STV1_YEAST STV1_YEAST]] Subunit of the integral membrane V0 complex of vacuolar ATPase essential for assembly and catalytic activity. Is present only in Golgi- and endosome-residing V-ATPase complexes. Enzymes containing this subunit have a 4-fold lower ratio of proton transport to ATP hydrolysis than complexes containing the vacuolar isoform and do not dissociate V1 and V0 in response to glucose depletion. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.<ref>PMID:11278748</ref> <ref>PMID:7514599</ref> [[http://www.uniprot.org/uniprot/VA0D_YEAST VA0D_YEAST]] Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. The active enzyme consists of a catalytic V1 domain attached to an integral membrane V0 proton pore complex. This subunit is a non-integral membrane component of the membrane pore domain and is required for proper assembly of the V0 sector. Might be involved in the regulated assembly of V1 subunits onto the membrane sector or alternatively may prevent the passage of protons through V0 pores. [[http://www.uniprot.org/uniprot/VATL2_YEAST VATL2_YEAST]] Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.<ref>PMID:1837023</ref> <ref>PMID:9030535</ref> [[http://www.uniprot.org/uniprot/VA0E_YEAST VA0E_YEAST]] Subunit of the integral membrane V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.<ref>PMID:14594803</ref> [[http://www.uniprot.org/uniprot/VATH_YEAST VATH_YEAST]] Vacuolar ATPases regulate the organelle acidity. This subunit is essential for activity, but not assembly, of the enzyme complex. [[http://www.uniprot.org/uniprot/VOA1_YEAST VOA1_YEAST]] Functions with VMA21 in assembly of the integral membrane sector (also called V0 complex) of the V-ATPase in the endoplasmic reticulum.<ref>PMID:18799613</ref> [[http://www.uniprot.org/uniprot/VATB_YEAST VATB_YEAST]] Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-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.<ref>PMID:2141385</ref>
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[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>
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==See Also==
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*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Beilsten-Edmands, V]]
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[[Category: Saccharomyces cerevisiae RM11-1a]]
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[[Category: Bueler, S A]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Robinson, C V]]
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[[Category: Beilsten-Edmands V]]
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[[Category: Rubinstein, J L]]
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[[Category: Bueler SA]]
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[[Category: Vasanthakumar, T]]
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[[Category: Robinson CV]]
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[[Category: Wu, D]]
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[[Category: Rubinstein JL]]
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[[Category: Membrane protein]]
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[[Category: Vasanthakumar T]]
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[[Category: Proton pump]]
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[[Category: Wu D]]

Current revision

Saccharomyces cerevisiae V-ATPase Stv1-V1VO State 3

6o7x, resolution 8.70Å

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