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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/VATA_THET8 VATA_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type alpha chain is a catalytic subunit. | | [https://www.uniprot.org/uniprot/VATA_THET8 VATA_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type alpha chain is a catalytic subunit. |
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| == Publication Abstract from PubMed ==
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| Rotary ATPases couple ATP synthesis or hydrolysis to proton translocation across a membrane. However, understanding proton translocation has been hampered by a lack of structural information for the membrane-embedded a subunit. The V/A-ATPase from the eubacteriumThermus thermophilusis similar in structure to the eukaryotic V-ATPase but has a simpler subunit composition and functions in vivo to synthesize ATP rather than pump protons. We determined theT. thermophilusV/A-ATPase structure by cryo-EM at 6.4 A resolution. Evolutionary covariance analysis allowed tracing of the a subunit sequence within the map, providing a complete model of the rotary ATPase. Comparing the membrane-embedded regions of theT. thermophilusV/A-ATPase and eukaryotic V-ATPase fromSaccharomyces cerevisiaeallowed identification of the alpha-helices that belong to the a subunit and revealed the existence of previously unknown subunits in the eukaryotic enzyme. Subsequent evolutionary covariance analysis enabled construction of a model of the a subunit in theS. cerevisaeV-ATPase that explains numerous biochemical studies of that enzyme. Comparing the two a subunit structures determined here with a structure of the distantly related a subunit from the bovine F-type ATP synthase revealed a conserved pattern of residues, suggesting a common mechanism for proton transport in all rotary ATPases.
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| Models for the a subunits of the Thermus thermophilus V/A-ATPase and Saccharomyces cerevisiae V-ATPase enzymes by cryo-EM and evolutionary covariance.,Schep DG, Zhao J, Rubinstein JL Proc Natl Acad Sci U S A. 2016 Mar 22;113(12):3245-50. doi:, 10.1073/pnas.1521990113. Epub 2016 Mar 7. PMID:26951669<ref>PMID:26951669</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 5gar" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[ATPase 3D structures|ATPase 3D structures]] | | *[[ATPase 3D structures|ATPase 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </SX> | | </SX> |