8yy1: Difference between revisions
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==Vo domain of V/A-ATPase from Thermus thermophilus state3== | |||
<StructureSection load='8yy1' size='340' side='right'caption='[[8yy1]], [[Resolution|resolution]] 3.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8yy1]] 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=8YY1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8YY1 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]] 3.6Å</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=8yy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8yy1 OCA], [https://pdbe.org/8yy1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8yy1 RCSB], [https://www.ebi.ac.uk/pdbsum/8yy1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8yy1 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. | |||
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 8yy1" style="background-color:#fffaf0;"></div> | ||
[[Category: Kishikawa | == References == | ||
[[Category: | <references/> | ||
[[Category: Nishida | __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
Vo domain of V/A-ATPase from Thermus thermophilus state3Vo domain of V/A-ATPase from Thermus thermophilus state3
Structural highlights
FunctionVATC_THET8 Produces ATP from ADP in the presence of a proton gradient across the membrane. Publication 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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