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| | <SX load='6c6l' size='340' side='right' viewer='molstar' caption='[[6c6l]], [[Resolution|resolution]] 3.50Å' scene=''> | | <SX load='6c6l' size='340' side='right' viewer='molstar' caption='[[6c6l]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6c6l]] is a 15 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C6L OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6C6L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6c6l]] 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=6C6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6C6L FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </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]] 3.5Å</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=6c6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c6l OCA], [http://pdbe.org/6c6l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c6l RCSB], [http://www.ebi.ac.uk/pdbsum/6c6l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c6l 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=6c6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c6l OCA], [https://pdbe.org/6c6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6c6l RCSB], [https://www.ebi.ac.uk/pdbsum/6c6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6c6l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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/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/VPH1_YEAST VPH1_YEAST]] Subunit of the integral membrane V0 complex of vacuolar ATPase essential for assembly and catalytic activity. 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. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.<ref>PMID:11278748</ref> <ref>PMID:1491220</ref> <ref>PMID:8798414</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/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/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. | + | [https://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> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | The molecular mechanism of transmembrane proton translocation in rotary motor ATPases is not fully understood. Here, we report the 3.5-A resolution cryoEM structure of the lipid nanodisc-reconstituted Vo proton channel of the yeast vacuolar H(+)-ATPase, captured in a physiologically relevant, autoinhibited state. The resulting atomic model provides structural detail for the amino acids that constitute the proton pathway at the interface of the proteolipid ring and subunit a. Based on the structure and previous mutagenesis studies, we propose the chemical basis of transmembrane proton transport. Moreover, we discovered that the C terminus of the assembly factor Voa1 is an integral component of mature Vo. Voa1's C-terminal transmembrane alpha helix is bound inside the proteolipid ring, where it contributes to the stability of the complex. Our structure rationalizes possible mechanisms by which mutations in human Vo can result in disease phenotypes and may thus provide new avenues for therapeutic interventions.
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| - | | + | |
| - | The 3.5-A CryoEM Structure of Nanodisc-Reconstituted Yeast Vacuolar ATPase Vo Proton Channel.,Roh SH, Stam NJ, Hryc CF, Couoh-Cardel S, Pintilie G, Chiu W, Wilkens S Mol Cell. 2018 Mar 15;69(6):993-1004.e3. doi: 10.1016/j.molcel.2018.02.006. Epub , 2018 Mar 8. PMID:29526695<ref>PMID:29526695</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
| + | |
| - | <div class="pdbe-citations 6c6l" style="background-color:#fffaf0;"></div>
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| | | | |
| | ==See Also== | | ==See Also== |
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| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chiu, W]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Couoh-Cardel, S]] | + | [[Category: Chiu W]] |
| - | [[Category: Hryc, C]] | + | [[Category: Couoh-Cardel S]] |
| - | [[Category: Pintilie, G]] | + | [[Category: Hryc C]] |
| - | [[Category: Roh, S]] | + | [[Category: Pintilie G]] |
| - | [[Category: Stam, N J]] | + | [[Category: Roh S]] |
| - | [[Category: Wilkens, S]] | + | [[Category: Stam NJ]] |
| - | [[Category: Membrane protein]]
| + | [[Category: Wilkens S]] |
| - | [[Category: Rotary motor enzyme]]
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| - | [[Category: Vacuolar h+-atpase]]
| + | |
| - | [[Category: Vo proton channel]]
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