Structure of ATP synthase from ESKAPE pathogen <i>Acinetobacter baumannii</i>.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 35171679.
- Also identified by DOI 10.1126/sciadv.abl5966 and PMC identifier 8849298.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
The global spread of multidrug-resistant <i>Acinetobacter baumannii</i> infections urgently calls for the identification of novel drug targets. We solved the electron cryo-microscopy structure of the F<sub>1</sub>F<sub>o</sub>-adenosine 5'-triphosphate (ATP) synthase from <i>A. baumannii</i> in three distinct conformational states. The nucleotide-converting F<sub>1</sub> subcomplex reveals a specific self-inhibition mechanism, which supports a unidirectional ratchet mechanism to avoid wasteful ATP consumption. In the membrane-embedded F<sub>o</sub> 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.
Medical subject headings
- Acinetobacter baumannii