8yxz: Difference between revisions

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-'''Unreleased structure'''
-The entry 8yxz is ON HOLD  until Paper Publication
+==Vo domain of V/A-ATPase from Thermus thermophilus state1==
+<StructureSection load='8yxz' size='340' side='right'caption='[[8yxz]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8yxz]] 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=8YXZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8YXZ 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&#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=8yxz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8yxz OCA], [https://pdbe.org/8yxz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8yxz RCSB], [https://www.ebi.ac.uk/pdbsum/8yxz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8yxz 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 state1
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Nishida, Y]]
+<div class="pdbe-citations 8yxz" style="background-color:#fffaf0;"></div>
-[[Category: Yokoyama, K]]
+== References ==
-[[Category: Nakano, A]]
+<references/>
-[[Category: Kishikawa, J]]
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Thermus thermophilus HB8]]
+[[Category: Kishikawa J]]
+[[Category: Nakano A]]
+[[Category: Nishida Y]]
+[[Category: Yokoyama K]]