View source for 8spw


==PS3 F1 Rotorless, low ATP==
<StructureSection load='8spw' size='340' side='right'caption='[[8spw]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8spw]] is a 6 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=8SPW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SPW 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]] 3.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=8spw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8spw OCA], [https://pdbe.org/8spw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8spw RCSB], [https://www.ebi.ac.uk/pdbsum/8spw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8spw 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 interchanges phosphate transfer energy and proton motive force via a rotary catalytic mechanism and isolated F(1)-ATPase subcomplexes can also hydrolyze ATP to generate rotation of their central gamma rotor subunit. As ATP is hydrolyzed, the F(1)-ATPase cycles through a series of conformational states that mediates unidirectional rotation of the rotor. However, even in the absence of a rotor, the alpha and beta subunits are still able to pass through a series of conformations, akin to those that generate rotation. Here, we use cryoelectron microscopy to establish the structures of these rotorless states. These structures indicate that cooperativity in this system is likely mediated by contacts between the beta subunit lever domains, irrespective of the presence of the gamma rotor subunit. These findings provide insight into how long-range information may be transferred in large biological systems.

The series of conformational states adopted by rotorless F(1)-ATPase during its hydrolysis cycle.,Sobti M, Ueno H, Brown SHJ, Noji H, Stewart AG Structure. 2024 Apr 4;32(4):393-399.e3. doi: 10.1016/j.str.2023.12.014. Epub 2024 , Jan 17. PMID:38237595<ref>PMID:38237595</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8spw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bacillus sp. PS3]]
[[Category: Large Structures]]
[[Category: Sobti M]]
[[Category: Stewart AG]]