Biophysics and bioinformatics reveal structural differences of the two peripheral stalk subunits in chloroplast ATP synthase.

ATP synthases convert an electrochemical proton gradient into rotational movement to produce the ubiquitous energy currency adenosine triphosphate. Tension generated by the rotational torque is compensated by the stator. For this task, a peripheral stalk flexibly fixes the hydrophilic catalytic part F1 to the membrane integral proton conducting part F(O) of the ATP synthase.

Does F1-ATPase subunit gamma turn in the wrong direction?

Analyzing the direction of F1-ATPase subunit gamma rotation, its shape and non-random distribution of surface residues, a mechanism is proposed for how gamma induces the closing/opening of the catalytic sites at beta/alpha interfaces: by keeping contact with the mobile domain of subunits beta at the 'jaw' (D386, the seven consecutive hydrophobic residues and D394/E395), rotating gamma works as a screw conveyer within the barrel of (alpha,beta)3. Mutations of the conveyer contacts are predicted to inhibit. Rotating wheel cartoons illustrate enzyme turnover and conformational changes.