7P2Y

F1Fo-ATP synthase from Acinetobacter baumannii (state 1)

Summary for 7P2Y

• Entry DOI: 10.2210/pdb7p2y/pdb
• EMDB information: 13174
• Descriptor: ATP synthase subunit alpha, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (13 entities in total)
• Functional Keywords: atp synthase, eskape, rotary atp synthase, f1fo, peptidisc, bioenergetics, imp, multi-drug resistance, pathogenic, membrane protein
• Biological source: Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377); More
• Total number of polymer chains: 22
• Total formula weight: 535809.15

Authors

Demmer, J.K.,Phillips, B.P.,Uhrig, O.L.,Filloux, A.,Allsopp, L.P.,Bublitz, M.,Meier, T. (deposition date: 2021-07-06, release date: 2022-02-02, Last modification date: 2024-07-17)

Primary citation

Demmer, J.K.,Phillips, B.P.,Uhrig, O.L.,Filloux, A.,Allsopp, L.P.,Bublitz, M.,Meier, T.
Structure of ATP synthase from ESKAPE pathogen Acinetobacter baumannii.
Sci Adv, 8:eabl5966-eabl5966, 2022

PubMed Abstract: The global spread of multidrug-resistant infections urgently calls for the identification of novel drug targets. We solved the electron cryo-microscopy structure of the FF-adenosine 5'-triphosphate (ATP) synthase from in three distinct conformational states. The nucleotide-converting F subcomplex reveals a specific self-inhibition mechanism, which supports a unidirectional ratchet mechanism to avoid wasteful ATP consumption. In the membrane-embedded F 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.

PubMed: 35171679
DOI: 10.1126/sciadv.abl5966

Experimental method

ELECTRON MICROSCOPY (3.1 Å)