Mitochondrial F1Fo-ATP synthase: the small subunits e and g associate with monomeric complexes to trigger dimerization.

@article{Wagner2009MitochondrialFS,
  title={Mitochondrial F1Fo-ATP synthase: the small subunits e and g associate with monomeric complexes to trigger dimerization.},
  author={Karina Wagner and Peter Rehling and Luiza K. Sanju{\'a}n Szklarz and Rebecca D. Taylor and Nikolaus Pfanner and Martin van der Laan},
  journal={Journal of molecular biology},
  year={2009},
  volume={392 4},
  pages={855-61}
}
Mitochondrial F(1)F(o)-ATP synthase catalyzes the formation of ATP from ADP and inorganic phosphate. The enzyme is found in monomeric, dimeric and higher oligomeric forms in the inner mitochondrial membrane. Dimerization of ATP synthase complexes is a prerequisite for the generation of larger oligomers that promote membrane bending and formation of tubular cristae membranes. Two small proteins of the membrane-embedded F(o)-domain, subunit e (Su e; Atp21) and Su g (Atp20), were identified as… CONTINUE READING