Two rotary motors in F-ATP synthase are elastically coupled by a flexible rotor and a stiff stator stalk.

ABSTRACT: ATP is synthesized by ATP synthase (F(O)F(1)-ATPase). Its rotary electromotor (F(O)) translocates protons (in some organisms sodium cations) and generates torque to drive the rotary chemical generator (F(1)). Elastic power transmission between F(O) and F(1) is essential for smoothing the cooperation of these stepping motors, thereby increasing their kinetic efficiency. A particularly compliant elastic domain is located on the central rotor (c(10-15)/ε/γ), right between the two sites of torque generation and consumption. The hinge on the active lever on subunit β adds further compliance. It is under contention whether or not the peripheral stalk (and the "stator" as a whole) also serves as elastic buffer. In the enzyme from Escherichia coli, the most extended component of the stalk is the h

SUBMITTER: Wachter A 

PROVIDER: S-EPMC3053995 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature