Extrinsic conditions influence the self-association and structure of IF₁, the regulatory protein of mitochondrial ATP synthase.

ABSTRACT: The endogenous inhibitor of ATP synthase in mitochondria, called IF₁, conserves cellular energy when the proton-motive force collapses by inhibiting ATP hydrolysis. Around neutrality, the 84-amino-acid bovine IF₁ is thought to self-assemble into active dimers and, under alkaline conditions, into inactive tetramers and higher oligomers. Dimerization is mediated by formation of an antiparallel α-helical coiled-coil involving residues 44-84. The inhibitory region of each monomer from residues 1-46 is largely α-helical in crystals, but disordered in solution. The formation of the inhibited enzyme complex requires the hydrolysis of two ATP molecules, and in the complex the disordered region from residues 8-13 is extended and is followed by an α-helix from residues 14-18 an

SUBMITTER: Boreikaite V 

PROVIDER: S-EPMC6535023 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature