Characterization of the flexibility of the peripheral stalk of prokaryotic rotary A-ATPases by atomistic simulations.

ABSTRACT: Rotary ATPases are involved in numerous physiological processes, with the three distinct types (F/A/V-ATPases) sharing functional properties and structural features. The basic mechanism involves the counter rotation of two motors, a soluble ATP hydrolyzing/synthesizing domain and a membrane-embedded ion pump connected through a central rotor axle and a stator complex. Within the A/V-ATPase family conformational flexibility of the EG stators has been shown to accommodate catalytic cycling and is considered to be important to function. For the A-ATPase three EG structures have been reported, thought to represent conformational states of the stator during different stages of rotary catalysis. Here we use long, detailed atomistic simulations to show that those structures are conformers explore

SUBMITTER: Papachristos K 

PROVIDER: S-EPMC4988496 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature