Dissecting the role of the γ-subunit in the rotary-chemical coupling and torque generation of F1-ATPase.

ABSTRACT: Unraveling the molecular nature of the conversion of chemical energy (ATP hydrolysis in the α/β-subunits) to mechanical energy and torque (rotation of the γ-subunit) in F1-ATPase is very challenging. A major part of the challenge involves understanding the rotary-chemical coupling by a nonphenomenological structure-energy description, while accounting for the observed torque generated on the γ-subunit and its change due to mutation of this unit. Here we extend our previous study that used a coarse-grained model of the F1-ATPase to generate a structure-based free energy landscape of the rotary-chemical process. Our quantitative analysis of the landscape reproduced the observed torque for the wild-type enzyme. In doing so, we found that there are several possibilities of torque generation fr

SUBMITTER: Mukherjee S 

PROVIDER: S-EPMC4352810 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature