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==== | ==The membrane-embedded Vo domain of V/A-ATPase from Thermus thermophilus== | ||
<StructureSection load='6ly9' size='340' side='right'caption='[[6ly9]]' scene=''> | <StructureSection load='6ly9' size='340' side='right'caption='[[6ly9]], [[Resolution|resolution]] 3.93Å' 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= OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6ly9]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LY9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LY9 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.93Å</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=6ly9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ly9 OCA], [https://pdbe.org/6ly9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ly9 RCSB], [https://www.ebi.ac.uk/pdbsum/6ly9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ly9 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5SIT6_THET8 Q5SIT6_THET8] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
V-ATPase is an energy converting enzyme, coupling ATP hydrolysis/synthesis in the hydrophilic V1 domain, with proton flow through the Vo membrane domain, via rotation of the central rotor complex relative to the surrounding stator apparatus. Upon dissociation from the V1 domain, the Vo domain of the eukaryotic V-ATPase can adopt a physiologically relevant auto-inhibited form in which proton conductance through the Vo domain is prevented, however the molecular mechanism of this inhibition is not fully understood. Using cryo-electron microscopy, we determined the structure of both the holo V/A-ATPase and isolated Vo at near-atomic resolution, respectively. These structures clarify how the isolated Vo domain adopts the auto-inhibited form and how the holo complex prevents formation of the inhibited Vo form. | |||
Mechanical inhibition of isolated Vo from V/A-ATPase for proton conductance.,Kishikawa JI, Nakanishi A, Furuta A, Kato T, Namba K, Tamakoshi M, Mitsuoka K, Yokoyama K Elife. 2020 Jul 8;9. pii: 56862. doi: 10.7554/eLife.56862. PMID:32639230<ref>PMID:32639230</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ly9" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermus thermophilus HB8]] | ||
[[Category: Furuta A]] | |||
[[Category: Kato T]] | |||
[[Category: Kishikawa J]] | |||
[[Category: Mitsuoka K]] | |||
[[Category: Nakanishi A]] | |||
[[Category: Namba K]] | |||
[[Category: Tamakoshi M]] | |||
[[Category: Yokoyama K]] | |||
Latest revision as of 11:07, 17 October 2024
The membrane-embedded Vo domain of V/A-ATPase from Thermus thermophilusThe membrane-embedded Vo domain of V/A-ATPase from Thermus thermophilus
Structural highlights
FunctionPublication Abstract from PubMedV-ATPase is an energy converting enzyme, coupling ATP hydrolysis/synthesis in the hydrophilic V1 domain, with proton flow through the Vo membrane domain, via rotation of the central rotor complex relative to the surrounding stator apparatus. Upon dissociation from the V1 domain, the Vo domain of the eukaryotic V-ATPase can adopt a physiologically relevant auto-inhibited form in which proton conductance through the Vo domain is prevented, however the molecular mechanism of this inhibition is not fully understood. Using cryo-electron microscopy, we determined the structure of both the holo V/A-ATPase and isolated Vo at near-atomic resolution, respectively. These structures clarify how the isolated Vo domain adopts the auto-inhibited form and how the holo complex prevents formation of the inhibited Vo form. Mechanical inhibition of isolated Vo from V/A-ATPase for proton conductance.,Kishikawa JI, Nakanishi A, Furuta A, Kato T, Namba K, Tamakoshi M, Mitsuoka K, Yokoyama K Elife. 2020 Jul 8;9. pii: 56862. doi: 10.7554/eLife.56862. PMID:32639230[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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