ATP binding by an F₁F_o ATP synthase ε subunit is pH dependent, suggesting a diversity of ε subunit functional regulation in bacteria.

ABSTRACT: It is a conjecture that the ε subunit regulates ATP hydrolytic function of the F₁F_o ATP synthase in bacteria. This has been proposed by the ε subunit taking an extended conformation, with a terminal helix probing into the central architecture of the hexameric catalytic domain, preventing ATP hydrolysis. The ε subunit takes a contracted conformation when bound to ATP, thus would not interfere with catalysis. A recent crystallographic study has disputed this; the Caldalkalibacillus thermarum TA2.A1 F₁F_o ATP synthase cannot natively hydrolyse ATP, yet studies have demonstrated that the loss of the ε subunit terminal helix results in an ATP synthase capable of ATP hydrolysis, supporting ε subunit function. Analysis of sequence and crystallogra

SUBMITTER: Krah A 

PROVIDER: S-EPMC10010621 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature