Structure and mechanism of the ATP synthase membrane motor inferred from quantitative integrative modeling.

ABSTRACT: Two subunits within the transmembrane domain of the ATP synthase-the c-ring and subunit a-energize the production of 90% of cellular ATP by transducing an electrochemical gradient of H⁺ or Na⁺ into rotational motion. The nature of this turbine-like energy conversion mechanism has been elusive for decades, owing to the lack of definitive structural information on subunit a or its c-ring interface. In a recent breakthrough, several structures of this complex were resolved by cryo-electron microscopy (cryo-EM), but the modest resolution of the data has led to divergent interpretations. Moreover, the unexpected architecture of the complex has cast doubts on a wealth of earlier biochemical analyses conducted to probe this structure. Here, we use quantitative molecular-mode

SUBMITTER: Leone V 

PROVIDER: S-EPMC5129741 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature