Cryo-EM reveals transition states of the Acinetobacter baumannii F₁-ATPase rotary subunits γ and ε, unveiling novel compound targets.

ABSTRACT: Priority 1: critical WHO pathogen Acinetobacter baumannii depends on ATP synthesis and ATP:ADP homeostasis and its bifunctional F₁F_O-ATP synthase. While synthesizing ATP, it regulates ATP cleavage by its inhibitory ε subunit to prevent wasteful ATP consumption. We determined cryo-electron microscopy structures of the ATPase active A. baumannii F₁-αßγε_Δ134-139 mutant in four distinct conformational states, revealing four transition states and structural transformation of the ε's C-terminal domain, forming the switch of an ATP hydrolysis off- and an ATP synthesis on-state based. These alterations go in concert with altered motions and interactions in the catalytic- and rotary subunits of this engine. These A. baumannii interacting sites provide nov

SUBMITTER: Le KCM 

PROVIDER: S-EPMC11580714 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature