View source for 9io5


==Cryo-EM structure of G1-ATPase dimer from Mycoplasma mobile gliding machinery==
<StructureSection load='9io5' size='340' side='right'caption='[[9io5]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9io5]] is a 26 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesomycoplasma_mobile Mesomycoplasma mobile]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9IO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9IO5 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]] 3.2&#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=9io5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9io5 OCA], [https://pdbe.org/9io5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9io5 RCSB], [https://www.ebi.ac.uk/pdbsum/9io5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9io5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6KIC8_MYCM1 Q6KIC8_MYCM1] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Rotary ATPases, including F(1)F(O)-, V(1)V(O)-, and A(1)A(O)-ATPases, are molecular motors that exhibit rotational movements for energy conversion. In the gliding bacterium, Mycoplasma mobile, a dimeric F(1)-like ATPase forms a chain structure within the cell, which is proposed to drive the gliding motility. However, the mechanisms of force generation and transmission remain unclear. We determined the electron cryomicroscopy (cryo-EM) structure of the dimeric F(1)-like ATPase complex. The structure revealed an assembly distinct from those of dimeric F(1)F(O)-ATPases. The F(1)-like ATPase unit associated by two subunits GliD and GliE was named G(1)-ATPase as an R(1) domain of rotary ATPases. G(1)-beta subunit, a homolog of the F(1)-ATPase catalytic subunit, exhibited a specific N-terminal region that incorporates the glycolytic enzyme, phosphoglycerate kinase into the complex. Structural features of the ATPase displayed strong similarities to F(1)-ATPase, suggesting a rotation based on the rotary catalytic mechanism. Overall, the cryo-EM structure provides insights into the mechanism through which G(1)-ATPase drives the Mycoplasma gliding motility.

Dimeric assembly of F(1)-like ATPase for the gliding motility of Mycoplasma.,Toyonaga T, Kato T, Kawamoto A, Miyata T, Kawakami K, Fujita J, Hamaguchi T, Namba K, Miyata M Sci Adv. 2025 Feb 28;11(9):eadr9319. doi: 10.1126/sciadv.adr9319. Epub 2025 Feb , 26. PMID:40009674<ref>PMID:40009674</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9io5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mesomycoplasma mobile]]
[[Category: Fujita J]]
[[Category: Hamaguchi T]]
[[Category: Kato T]]
[[Category: Kawakami K]]
[[Category: Kawamoto A]]
[[Category: Miyata M]]
[[Category: Miyata T]]
[[Category: Namba K]]
[[Category: Toyonaga T]]