24DJ
Structural snapshots of F1-ATPase catalysis in drug resistant Acinetobacter baumannii reveal novel therapeutic targets - Conformation 1b
Summary for 24DJ
| Entry DOI | 10.2210/pdb24dj/pdb |
| EMDB information | 69446 |
| Descriptor | ATP synthase subunit beta, ATP synthase subunit alpha, ATP synthase epsilon chain, ... (8 entities in total) |
| Functional Keywords | atp hydrolysis, f1-atpase, hydrolase |
| Biological source | Acinetobacter baumannii AB5075 More |
| Total number of polymer chains | 8 |
| Total formula weight | 366675.09 |
| Authors | |
| Primary citation | Le, K.C.M.,Marzinek, J.K.,Mathiyazakan, V.,Bond, P.J.,Gruber, G. Structural Snapshots of F 1 -ATPase Catalysis in Drug Resistant Acinetobacter baumannii Reveal Novel Therapeutic Targets. Faseb J., 40:e72385-e72385, 2026 Cited by PubMed Abstract: Gram-negative Acinetobacter baumannii, one of the most critical priority pathogens, has developed multiple defense mechanisms, including upregulation of drug efflux pumps powered by the proton-motive force (pmf) or ATP. As a nonfermenting bacterium, it relies on oxidative phosphorylation, in which the F-ATP synthase, composed of an F-ATPase (α:β:γ:ε) and F-domain (a:b:c), synthesizes ATP, the cell's currency of life. Here, we present cryo-electron microscopy structures of the F-ATPase captured during ATP synthesis, revealing concerted conformational changes within the α:β-catalytic head that trigger structural transitions of subunit ε and twisting of the γ:ε central stalk, coupled with spontaneous ATP formation. Molecular dynamics simulations validate and expand the ensemble of structural rearrangements underlying the rotary mechanism. The resolved intermediate states of the ε subunit reveal its role as a molecular gear, regulating ATP synthesis while simultaneously inhibiting ATP hydrolysis, essential for the pathogen to prevent wastage of ATP. These structural snapshots identify novel therapeutic targets and pave the way for rational design of selective inhibitors. PubMed: 42891652DOI: 10.1096/fj.202602735R PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.24 Å) |
Structure validation
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