Molecular Structure and Rotary Dynamics of Enterococcus hirae V-1-ATPase

摘要

V-1-ATPase is a rotary molecular motor in which the mechanical rotation of the rotor DF subunits against the stator A(3)B(3) ring is driven by the chemical free energy of ATP hydrolysis. Recently, using X-ray crystallography, we solved the high-resolution molecular structure of Enterococcus hirae V-1-ATPase (EhV(1)) and revealed how the three catalytic sites in the stator A(3)B(3) ring change their structure on nucleotide binding and interaction with the rotor DF subunits. Furthermore, recently, we also demonstrated directly the rotary catalysis of EhV(1) by using single-molecule high-speed imaging and analyzed the properties of the rotary motion in detail. In this critical review, we introduce the molecular structure and rotary dynamics of EhV(1) and discuss a possible model of its chemomechanical coupling scheme. (c) 2014 IUBMB Life, 66(9):624-630, 2014