The phototroph-specific β-hairpin structure of the γ subunit of F_oF₁-ATP synthase is important for efficient ATP synthesis of cyanobacteria.

ABSTRACT: The F_oF₁ synthase produces ATP from ADP and inorganic phosphate. The γ subunit of F_oF₁ ATP synthase in photosynthetic organisms, which is the rotor subunit of this enzyme, contains a characteristic β-hairpin structure. This structure is formed from an insertion sequence that has been conserved only in phototrophs. Using recombinant subcomplexes, we previously demonstrated that this region plays an essential role in the regulation of ATP hydrolysis activity, thereby functioning in controlling intracellular ATP levels in response to changes in the light environment. However, the role of this region in ATP synthesis has long remained an open question because its analysis requires the preparation of the whole F_oF₁ complex and a

SUBMITTER: Kondo K 

PROVIDER: S-EPMC8390522 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature