9VKS
Cryo-EM structure of F-ATP synthase c-ring from Mycobacteroides abscessus (Backbone)
Summary for 9VKS
| Entry DOI | 10.2210/pdb9vks/pdb |
| EMDB information | 65141 |
| Descriptor | ATP synthase subunit c (1 entity in total) |
| Functional Keywords | hydrolase, atp synthase, membrane protein, mycobacterium abscessus, mycobacterial, c-ring, nontuberculous mycobacteria |
| Biological source | Mycobacteroides abscessus subsp. abscessus |
| Total number of polymer chains | 9 |
| Total formula weight | 73426.28 |
| Authors | Fong, T.C.,Saw, W.-G.,Mathiyazakan, V.,Wong, C.F.,Grueber, G. (deposition date: 2025-06-23, release date: 2026-01-14) |
| Primary citation | Fong, T.C.,Saw, W.G.,Mathiyazakan, V.,Wong, C.F.,Gruber, G. The Mycobacterium abscessus F-ATP synthase structure reveals mechanistic elements enabling rational drug design to combat NTM lung disease. Structure, 2025 Cited by PubMed Abstract: 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 α-subunit extension involved in the inhibition of ATP hydrolysis, energy transmission via the γε-stalk, and mechanochemical coupling by the δ-subunit. The structural blueprint allows precise target engagement and optimization of hits-to-leads and existing anti-Mab inhibitors targeting the engine. PubMed: 41475343DOI: 10.1016/j.str.2025.12.005 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (5.61 Å) |
Structure validation
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