Figure 9: Proposed model of the rotation mechanism of Enterococcus hirae V1-ATPase.
From: Crystal structures of the ATP-binding and ADP-release dwells of the V1 rotary motor
(a–d) The structure models are based on the crystal structures of 2ATPV1 (catalytic dwell; a,d), 2ADPV1 (ATP-binding dwell; b), and 3ADPV1 (ADP-release dwell; c) determined in this study. ATP indicated as a yellow ‘P’ in (a) and (d) represents an ATP molecule that is committed to hydrolysis. (e) Correspondence table for all AB pairs observed in the crystal structures of the A3B3 and V1 complexes. See text for additional details.
