Mechanism of the αβ conformational change in F1-ATPase after ATP hydrolysis: free-energy simulations.

ABSTRACT: One of the motive forces for F1-ATPase rotation is the conformational change of the catalytically active β subunit due to closing and opening motions caused by ATP binding and hydrolysis, respectively. The closing motion is accomplished in two steps: the hydrogen-bond network around ATP changes and then the entire structure changes via B-helix sliding, as shown in our previous study. Here, we investigated the opening motion induced by ATP hydrolysis using all-atom free-energy simulations, combining the nudged elastic band method and umbrella sampling molecular-dynamics simulations. Because hydrolysis requires residues in the α subunit, the simulations were performed with the αβ dimer. The results indicate that the large-scale opening motion is also achieved by the B-helix sliding (in the r

SUBMITTER: Ito Y 

PROVIDER: S-EPMC4286612 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature