Referenced in: none

Automatically associated channels: Slo1

Title: Rotary ATPases: A New Twist to an Ancient Machine.

Authors: Werner Kühlbrandt, Karen M Davies

Journal, date & volume: Trends Biochem. Sci., 2016 Jan , 41, 106-16

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/26671611

Abstract
Rotary ATPases are energy-converting nanomachines found in the membranes of all living organisms. The mechanism by which proton translocation through the membrane drives ATP synthesis, or how ATP hydrolysis generates a transmembrane proton gradient, has been unresolved for decades because the structure of a critical subunit in the membrane was unknown. Electron cryomicroscopy (cryoEM) studies of two rotary ATPases have now revealed a hairpin of long, horizontal, membrane-intrinsic α-helices in the a-subunit next to the c-ring rotor. The horizontal helices create a pair of aqueous half-channels in the membrane that provide access to the proton-binding sites in the rotor ring. These recent findings help to explain the highly conserved mechanism of ion translocation by rotary ATPases.