Mutational analysis of a conserved positive charge in the c-ring of E. coli ATP synthase.

ABSTRACT: F₁F_o ATP synthase is a ubiquitous molecular motor that utilizes a rotary mechanism to synthesize adenosine triphosphate (ATP), the fundamental energy currency of life. The membrane-embedded F_o motor converts the electrochemical gradient of protons into rotation, which is then used to drive the conformational changes in the soluble F₁ motor that catalyze ATP synthesis. In E. coli, the F_o motor is composed of a c₁₀ ring (rotor) alongside subunit a (stator), which together provide two aqueous half channels that facilitate proton translocation. Previous work has suggested that Arg50 and Thr51 on the cytoplasmic side of each subunit c are involved in the proton translocation process, and positive charge is conserved in this regio

SUBMITTER: Shrestha RK 

PROVIDER: S-EPMC9998364 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature