8ywt: Difference between revisions
New page: '''Unreleased structure''' The entry 8ywt is ON HOLD Authors: Kishikawa, J., Nishida, Y., Nakano, A., Yokoyama, K. Description: The isolated Vo domain of V/A-ATPase from Thermus thermo... |
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The | ==The isolated Vo domain of V/A-ATPase from Thermus thermophilus.== | ||
<StructureSection load='8ywt' size='340' side='right'caption='[[8ywt]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8ywt]] 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=8YWT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8YWT FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.8Å</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=8ywt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ywt OCA], [https://pdbe.org/8ywt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ywt RCSB], [https://www.ebi.ac.uk/pdbsum/8ywt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ywt ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5SIT6_THET8 Q5SIT6_THET8] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
ATP synthases play a crucial role in energy production by utilizing the proton motive force (pmf) across the membrane to rotate their membrane-embedded rotor c-ring, and thus driving ATP synthesis in the hydrophilic catalytic hexamer. However, the mechanism of how pmf converts into c-ring rotation remains unclear. This study presents a 2.8 A cryo-EM structure of the V(o) domain of V/A-ATPase from Thermus thermophilus, revealing precise orientations of glutamate (Glu) residues in the c(12)-ring. Three Glu residues face a water channel, with one forming a salt bridge with the Arginine in the stator (a/Arg). Molecular dynamics (MD) simulations show that protonation of specific Glu residues triggers unidirectional Brownian motion of the c(12)-ring towards ATP synthesis. When the key Glu remains unprotonated, the salt bridge persists, blocking rotation. These findings suggest that asymmetry in the protonation of c/Glu residues biases c(12)-ring movement, facilitating rotation and ATP synthesis. | |||
Rotary mechanism of the prokaryotic V(o) motor driven by proton motive force.,Kishikawa JI, Nishida Y, Nakano A, Kato T, Mitsuoka K, Okazaki KI, Yokoyama K Nat Commun. 2024 Nov 20;15(1):9883. doi: 10.1038/s41467-024-53504-x. PMID:39567487<ref>PMID:39567487</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8ywt" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Nakano | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermus thermophilus HB8]] | |||
[[Category: Kishikawa J]] | |||
[[Category: Nakano A]] | |||
[[Category: Nishida Y]] | |||
[[Category: Yokoyama K]] | |||