Arrangement of subunits in intact mammalian mitochondrial ATP synthase determined by cryo-EM.

Lindsay A Baker, Ian N Watt, Michael J Runswick, John E Walker, John L Rubinstein

Proceedings of the National Academy of Sciences of the United States of America 2012 Jul 17

filter terms:

Mitochondrial ATP synthase is responsible for the synthesis of ATP, a universal energy currency in cells. Whereas X-ray crystallography has revealed the structure of the soluble region of the complex and the membrane-intrinsic c-subunits, little is known about the structure of the six other proteins (a, b, f, A6L, e, and g) that comprise the membrane-bound region of the complex in animal mitochondria. Here, we present the structure of intact bovine mitochondrial ATP synthase at ∼18 Å resolution by electron cryomicroscopy of single particles in amorphous ice. The map reveals that the a-subunit and c(8)-ring of the complex interact with a small contact area and that the b-subunit spans the membrane without contacting the c(8)-ring. The e- and g-subunits extend from the a-subunit density distal to the c(8)-ring. The map was calculated from images of a preparation of the enzyme solubilized with the detergent dodecyl maltoside, which is visible in electron cryomicroscopy maps. The structure shows that the micelle surrounding the complex is curved. The observed bend in the micelle of the detergent-solubilized complex is consistent with previous electron tomography experiments and suggests that monomers of ATP synthase are sufficient to produce curvature in lipid bilayers.

Citation

Lindsay A Baker, Ian N Watt, Michael J Runswick, John E Walker, John L Rubinstein. Arrangement of subunits in intact mammalian mitochondrial ATP synthase determined by cryo-EM. Proceedings of the National Academy of Sciences of the United States of America. 2012 Jul 17;109(29):11675-80