8ywt: Difference between revisions
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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: Kishikawa | == References == | ||
[[Category: Nishida | <references/> | ||
[[Category: Yokoyama | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermus thermophilus HB8]] | |||
[[Category: Kishikawa J]] | |||
[[Category: Nakano A]] | |||
[[Category: Nishida Y]] | |||
[[Category: Yokoyama K]] | |||
Latest revision as of 09:18, 4 December 2024
The isolated Vo domain of V/A-ATPase from Thermus thermophilus.The isolated Vo domain of V/A-ATPase from Thermus thermophilus.
Structural highlights
FunctionPublication Abstract from PubMedATP 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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