Structural highlights
Function
ATPA_ACIBT Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.[HAMAP-Rule:MF_01346]
Publication Abstract from PubMed
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 F(1)F(o)-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.
Structure of ATP synthase from ESKAPE pathogen Acinetobacter baumannii.,Demmer JK, Phillips BP, Uhrig OL, Filloux A, Allsopp LP, Bublitz M, Meier T Sci Adv. 2022 Feb 18;8(7):eabl5966. doi: 10.1126/sciadv.abl5966. Epub 2022 Feb , 16. PMID:35171679[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Demmer JK, Phillips BP, Uhrig OL, Filloux A, Allsopp LP, Bublitz M, Meier T. Structure of ATP synthase from ESKAPE pathogen Acinetobacter baumannii. Sci Adv. 2022 Feb 18;8(7):eabl5966. PMID:35171679 doi:10.1126/sciadv.abl5966
