Structure of ATP synthase from ESKAPE pathogen Acinetobacter baumannii

The global spread of multidrug-resistant Acinetobacter baumannii infections urgently calls for the identification of novel drug targets. We solved the electron cryo-microscopy structure of the F1Fo-adenosine 5'-triphosphate (ATP) synthase from A. baumannii in three distinct conformational states. The nucleotide-converting F-1 subcomplex reveals a specific self-inhibition mechanism, which supports a unidirectional ratchet mechanism to avoid wasteful ATP consumption. In the membrane-embedded F-o complex, the structure shows unique structural adaptations along both the entry and exit pathways of the proton-conducting a-subunit. These features, absent in mitochondrial ATP synthases, represent attractive targets for the development of next-generation therapeutics that can act directly at the culmination of bioenergetics in this clinically relevant pathogen.

Automated summary

This research elucidates the structure of F1Fo-ATP synthase in A. baumannii and reveals specific self-inhibition mechanism and structural adaptations in the proton-conducting pathway. These features may serve as attractive targets for the development of next-generation therapeutics.