In situ structure of trypanosomal ATP synthase dimer reveals a unique arrangement of catalytic subunits.

ABSTRACT: We used electron cryotomography and subtomogram averaging to determine the in situ structures of mitochondrial ATP synthase dimers from two organisms belonging to the phylum euglenozoa: Trypanosoma brucei, a lethal human parasite, and Euglena gracilis, a photosynthetic protist. At a resolution of 32.5 Å and 27.5 Å, respectively, the two structures clearly exhibit a noncanonical F₁ head, in which the catalytic (αβ)₃ assembly forms a triangular pyramid rather than the pseudo-sixfold ring arrangement typical of all other ATP synthases investigated so far. Fitting of known X-ray structures reveals that this unusual geometry results from a phylum-specific cleavage of the α subunit, in which the C-terminal α_C fragments are displaced by ∼20 Å and rotated by ∼30° f

SUBMITTER: Muhleip AW 

PROVIDER: S-EPMC5293049 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature