View source for 9vks


==Cryo-EM structure of F-ATP synthase c-ring from Mycobacteroides abscessus (Backbone)==
<StructureSection load='9vks' size='340' side='right'caption='[[9vks]], [[Resolution|resolution]] 5.61&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9vks]] is a 9 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=9VKS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9VKS 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]] 5.61&#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=9vks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9vks OCA], [https://pdbe.org/9vks PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9vks RCSB], [https://www.ebi.ac.uk/pdbsum/9vks PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9vks ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B1MLV7_MYCA9 B1MLV7_MYCA9] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.[ARBA:ARBA00025198][HAMAP-Rule:MF_01396]  Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396]
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== 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>
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== 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]]