View source for 9avj


==PS3 F1 ATPase Wild type==
<StructureSection load='9avj' size='340' side='right'caption='[[9avj]], [[Resolution|resolution]] 3.72&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9avj]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._PS3 Bacillus sp. PS3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9AVJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9AVJ 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]] 3.72&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=9avj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9avj OCA], [https://pdbe.org/9avj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9avj RCSB], [https://www.ebi.ac.uk/pdbsum/9avj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9avj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0M3VGF9_BACP3 A0A0M3VGF9_BACP3] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.[HAMAP-Rule:MF_01346]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
F(1)F(o) ATP synthase is a molecular rotary motor that can generate ATP using a transmembrane proton motive force. Isolated F(1)-ATPase catalytic cores can hydrolyse ATP, passing through a series of conformational states involving rotation of the central gamma rotor subunit and the opening and closing of the catalytic beta subunits. Cooperativity in F(1)-ATPase has long thought to be conferred through the gamma subunit, with three key interaction sites between the gamma and beta subunits being identified. Single molecule studies have demonstrated that the F(1) complexes lacking the gamma axle still "rotate" and hydrolyse ATP, but with less efficiency. We solved the cryogenic electron microscopy structure of an axle-less Bacillus sp. PS3 F(1)-ATPase. The unexpected binding-dwell conformation of the structure in combination with the observed lack of interactions between the axle-less gamma and the open beta subunit suggests that the complete gamma subunit is important for coordinating efficient ATP binding of F(1)-ATPase.

The molecular structure of an axle-less F(1)-ATPase.,Furlong EJ, Reininger-Chatzigiannakis IP, Zeng YC, Brown SHJ, Sobti M, Stewart AG Biochim Biophys Acta Bioenerg. 2024 Oct 18:149521. doi: , 10.1016/j.bbabio.2024.149521. PMID:39428050<ref>PMID:39428050</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9avj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus sp. PS3]]
[[Category: Large Structures]]
[[Category: Sobti M]]
[[Category: Stewart AG]]