View source for 9vkr


==Cryo-EM structure of F-ATP synthase from Mycobacteroides abscessus (Rotational State 3)==
<StructureSection load='9vkr' size='340' side='right'caption='[[9vkr]], [[Resolution|resolution]] 2.79&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9vkr]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacteroides_abscessus_subsp._abscessus Mycobacteroides abscessus subsp. abscessus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9VKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9VKR 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]] 2.79&#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></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=9vkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9vkr OCA], [https://pdbe.org/9vkr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9vkr RCSB], [https://www.ebi.ac.uk/pdbsum/9vkr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9vkr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ATPA_MYCA9 ATPA_MYCA9] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The increasing global incidence rate of nontuberculous mycobacteria pulmonary infections is an emerging public health crisis, with Mycobacterium abscessus (Mab) being one of the most virulent and treatment-refractory of these pathogens. Mab exhibits extensive intrinsic and acquired drug resistance mechanisms that neutralize most antimicrobials against this pathogen, causing a clinical conundrum. As Mab relies on oxidative phosphorylation as its main energy source, its essential F-ATP synthase is a promising drug target but remains poorly understood due to a lack of host expression systems. Here, we present the expression, isolation, and structural characterization of Mab's F-ATP synthase. Cryo-EM reveals three nucleotide-driven rotational states at atomic resolution, highlighting key catalytic centers, a mycobacteria-specific alpha-subunit extension involved in the inhibition of ATP hydrolysis, energy transmission via the gammaepsilon-stalk, and mechanochemical coupling by the delta-subunit. The structural blueprint allows precise target engagement and optimization of hits-to-leads and existing anti-Mab inhibitors targeting the engine.

The Mycobacterium abscessus F-ATP synthase structure reveals mechanistic elements enabling rational drug design to combat NTM lung disease.,Fong TC, Saw WG, Mathiyazakan V, Wong CF, Gruber G Structure. 2025 Dec 30:S0969-2126(25)00486-1. doi: 10.1016/j.str.2025.12.005. PMID:41475343<ref>PMID:41475343</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9vkr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacteroides abscessus subsp. abscessus]]
[[Category: Fong TC]]
[[Category: Grueber G]]
[[Category: Mathiyazakan V]]
[[Category: Saw W-G]]
[[Category: Wong CF]]