6o7x - Revision history

OCA at 09:23, 20 March 2024

2024-03-20T09:23:20Z

← Older revision		Revision as of 09:23, 20 March 2024
Line 3:		Line 3:
	<SX load='6o7x' size='340' side='right' viewer='molstar' caption='[[6o7x]], [[Resolution\|resolution]] 8.70Å' scene=''>		<SX load='6o7x' size='340' side='right' viewer='molstar' caption='[[6o7x]], [[Resolution\|resolution]] 8.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6o7x]] is a 31 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Baker's_yeast Baker's yeast~~] and [~~http~~://en.wikipedia.org/wiki/~~Saccharomyces_cerevisiae~~ Saccharomyces cerevisiae]. 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~~://proteopedia.org/fgij/fg.htm?mol=6O7X FirstGlance]. <br>		<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>
	</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>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 8.7Å</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=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>		<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 ==
	[[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/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/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/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/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/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/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/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/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/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/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/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/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/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>		[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>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Proton-translocating vacuolar-type ATPases (V-ATPases) are necessary for numerous processes in eukaryotic cells, including receptor-mediated endocytosis, protein maturation, and lysosomal acidification. In mammals, V-ATPase subunit isoforms are differentially targeted to various intracellular compartments or tissues, but how these subunit isoforms influence enzyme activity is not clear. In the yeast Saccharomyces cerevisiae, isoform diversity is limited to two different versions of the proton-translocating subunit a: Vph1p, which is targeted to the vacuole, and Stv1p, which is targeted to the Golgi apparatus and endosomes. We show that purified V-ATPase complexes containing Vph1p have higher ATPase activity than complexes containing Stv1p and that the relative difference in activity depends on the presence of lipids. We also show that VO complexes containing Stv1p could be readily purified without attached V1 regions. We used this effect to determine structures of the membrane-embedded VO region with Stv1p at 3.1-A resolution, which we compare with a structure of the VO region with Vph1p that we determine to 3.2-A resolution. These maps reveal differences in the surface charge near the cytoplasmic proton half-channel. Both maps also show the presence of bound lipids, as well as regularly spaced densities that may correspond to ergosterol or bound detergent, around the c-ring.

	Structural comparison of the vacuolar and Golgi V-ATPases from Saccharomyces cerevisiae.,Vasanthakumar T, Bueler SA, Wu D, Beilsten-Edmands V, Robinson CV, Rubinstein JL Proc Natl Acad Sci U S A. 2019 Mar 25. pii: 1814818116. doi:, 10.1073/pnas.1814818116. PMID:30910982<ref>PMID:30910982</ref>		==See Also==
			*[[ATPase 3D structures\|ATPase 3D structures]]
	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class~~=~~"pdbe-citations 6o7x" style~~=~~"background-color:#fffaf0;"></div>~~
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</SX>		</SX>
	~~[[Category: Baker's yeast]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
	[[Category: ~~Beilsten~~-~~Edmands, V~~]]		[[Category: Saccharomyces cerevisiae RM11-1a]]
	[[Category: ~~Bueler, S A~~]]		[[Category: Saccharomyces cerevisiae S288C]]
	[[Category: ~~Robinson, C~~ V]]		[[Category: Beilsten-Edmands V]]
	[[Category: ~~Rubinstein, J L~~]]		[[Category: Bueler SA]]
	[[Category: ~~Vasanthakumar, T~~]]		[[Category: Robinson CV]]
	[[Category: ~~Wu, D~~]]		[[Category: Rubinstein JL]]
	[[Category: ~~Membrane protein~~]]		[[Category: Vasanthakumar T]]
	[[Category: ~~Proton pump~~]]		[[Category: Wu D]]

OCA at 03:47, 11 April 2020

2020-04-11T03:47:38Z

← Older revision		Revision as of 03:47, 11 April 2020
Line 3:		Line 3:
	<SX load='6o7x' size='340' side='right' viewer='molstar' caption='[[6o7x]], [[Resolution\|resolution]] 8.70Å' scene=''>		<SX load='6o7x' size='340' side='right' viewer='molstar' caption='[[6o7x]], [[Resolution\|resolution]] 8.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6o7x]] is a 31 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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>		<table><tr><td colspan='2'>[[6o7x]] is a 31 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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://proteopedia.org/fgij/fg.htm?mol=6O7X FirstGlance]. <br>
	</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>		</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>
	<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>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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>
	</table>		</table>
	== Function ==		== Function ==
	[[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>		[[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/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/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/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/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/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/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/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/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/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/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/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/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/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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 23:08, 6 March 2020

2020-03-06T23:08:08Z

← Older revision		Revision as of 23:08, 6 March 2020
Line 1:		Line 1:

	==Saccharomyces cerevisiae V-ATPase Stv1-V1VO State 3==		==Saccharomyces cerevisiae V-ATPase Stv1-V1VO State 3==
	<~~StructureSection~~ load='6o7x' size='340' side='right'caption='[[6o7x]], [[Resolution\|resolution]] 8.70Å' scene=''>		<SX load='6o7x' size='340' side='right' viewer='molstar' caption='[[6o7x]], [[Resolution\|resolution]] 8.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6o7x]] is a 31 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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>		<table><tr><td colspan='2'>[[6o7x]] is a 31 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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>
Line 21:		Line 21:
	<references/>		<references/>
	__TOC__		__TOC__
	</~~StructureSection~~>		</SX>
	[[Category: Baker's yeast]]		[[Category: Baker's yeast]]
	[[Category: Large Structures]]		[[Category: Large Structures]]

OCA at 08:00, 10 April 2019

2019-04-10T08:00:44Z

← Older revision		Revision as of 08:00, 10 April 2019
Line 3:		Line 3:
	<StructureSection load='6o7x' size='340' side='right'caption='[[6o7x]], [[Resolution\|resolution]] 8.70Å' scene=''>		<StructureSection load='6o7x' size='340' side='right'caption='[[6o7x]], [[Resolution\|resolution]] 8.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<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>		<table><tr><td colspan='2'>[[6o7x]] is a 31 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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>
	</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>		</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>
	<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>		<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>
Line 9:		Line 9:
	== Function ==		== Function ==
	[[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>		[[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>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Proton-translocating vacuolar-type ATPases (V-ATPases) are necessary for numerous processes in eukaryotic cells, including receptor-mediated endocytosis, protein maturation, and lysosomal acidification. In mammals, V-ATPase subunit isoforms are differentially targeted to various intracellular compartments or tissues, but how these subunit isoforms influence enzyme activity is not clear. In the yeast Saccharomyces cerevisiae, isoform diversity is limited to two different versions of the proton-translocating subunit a: Vph1p, which is targeted to the vacuole, and Stv1p, which is targeted to the Golgi apparatus and endosomes. We show that purified V-ATPase complexes containing Vph1p have higher ATPase activity than complexes containing Stv1p and that the relative difference in activity depends on the presence of lipids. We also show that VO complexes containing Stv1p could be readily purified without attached V1 regions. We used this effect to determine structures of the membrane-embedded VO region with Stv1p at 3.1-A resolution, which we compare with a structure of the VO region with Vph1p that we determine to 3.2-A resolution. These maps reveal differences in the surface charge near the cytoplasmic proton half-channel. Both maps also show the presence of bound lipids, as well as regularly spaced densities that may correspond to ergosterol or bound detergent, around the c-ring.

			Structural comparison of the vacuolar and Golgi V-ATPases from Saccharomyces cerevisiae.,Vasanthakumar T, Bueler SA, Wu D, Beilsten-Edmands V, Robinson CV, Rubinstein JL Proc Natl Acad Sci U S A. 2019 Mar 25. pii: 1814818116. doi:, 10.1073/pnas.1814818116. PMID:30910982<ref>PMID:30910982</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 6o7x" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Baker's yeast]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]

OCA at 07:13, 3 April 2019

2019-04-03T07:13:22Z

@@ Line 1: / Line 1: @@
-The entry 6o7x is ON HOLD
+==Saccharomyces cerevisiae V-ATPase Stv1-V1VO State 3==
+<StructureSection load='6o7x' size='340' side='right'caption='[[6o7x]], [[Resolution|resolution]] 8.70&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<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>
-Description:
+</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>
-[[Category: Unreleased Structures]]
+<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>

OCA: Protected "6o7x" [edit=sysop:move=sysop]

2019-03-20T05:57:34Z

Protected "6o7x" [edit=sysop:move=sysop]

← Older revision	Revision as of 05:57, 20 March 2019
(No difference)

OCA: New page: '''Unreleased structure''' The entry 6o7x is ON HOLD Authors: Description: Category: Unreleased Structures

2019-03-20T05:57:32Z

New page: '''Unreleased structure''' The entry 6o7x is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6o7x is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]