8yy0: Difference between revisions

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'''Unreleased structure'''


The entry 8yy0 is ON HOLD  until Paper Publication
==Vo domain of V/A-ATPase from Thermus thermophilus state2==
<StructureSection load='8yy0' size='340' side='right'caption='[[8yy0]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8yy0]] is a 14 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=8YY0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8YY0 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]] 3.6&#8491;</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=8yy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8yy0 OCA], [https://pdbe.org/8yy0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8yy0 RCSB], [https://www.ebi.ac.uk/pdbsum/8yy0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8yy0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VATC_THET8 VATC_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane.
<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.


Authors: Kishikawa, J., Nishida, Y., Nakano, A., Yokoyama, K.
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>


Description: Vo domain of V/A-ATPase from Thermus thermophilus state2
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Kishikawa, J]]
<div class="pdbe-citations 8yy0" style="background-color:#fffaf0;"></div>
[[Category: Nakano, A]]
== References ==
[[Category: Yokoyama, K]]
<references/>
[[Category: Nishida, Y]]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus thermophilus HB8]]
[[Category: Kishikawa J]]
[[Category: Nakano A]]
[[Category: Nishida Y]]
[[Category: Yokoyama K]]
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