Atomic model for the dimeric F O region of mitochondrial ATP synthase

• DOI: 10.1126/science.aao4815
• Publication Date: 2017-10-26T18:00:58Z
• Authors: Hui Guo; Stephanie A. Bueler; John L. Rubinstein
• Keywords: Models, Molecular; 0301 basic medicine; Protein Folding; 03 medical and health sciences; Saccharomyces cerevisiae Proteins; Cryoelectron Microscopy; Saccharomyces cerevisiae; Mitochondrial Proton-Translocating ATPases; Protein Multimerization; Crystallography, X-Ray; Protein Structure, Secondary; Mitochondria

How protons power rotation

Synthesis of adenosine triphosphate (ATP) in mitochondria is accomplished by a large molecular machine, the F 1 F O ATP synthase. Proton translocation across the F O region that spans the mitochondrial inner membrane drives ATP synthesis in the F 1 region through a rotational mechanism. Guo et al. present a high-resolution structure of the dimeric F O complex from Saccharomyces cerevisiae , determined by electron microscopy. The structure gives insights into how proton translocation powers rotation and suggests how F O dimers bend the membrane to give mitochondria their characteristic cristae.

Science , this issue p. 936