ATP synthase from <i>Trypanosoma brucei</i> has an elaborated canonical F₁-domain and conventional catalytic sites.

ABSTRACT: The structures and functions of the components of ATP synthases, especially those subunits involved directly in the catalytic formation of ATP, are widely conserved in metazoans, fungi, eubacteria, and plant chloroplasts. On the basis of a map at 32.5-Å resolution determined in situ in the mitochondria of Trypanosoma brucei by electron cryotomography, it has been proposed that the ATP synthase in this species has a noncanonical structure and different catalytic sites in which the catalytically essential arginine finger is provided not by the α-subunit adjacent to the catalytic nucleotide-binding site as in all species investigated to date, but rather by a protein, p18, found only in the euglenozoa. A crystal structure at 3.2-Å resolution of the catalytic domain of the same enzyme de

SUBMITTER: Montgomery MG 

PROVIDER: S-EPMC5834723 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature