Paper Citing NAMD - Abstract
Liu, Ming S.; Todd, B. D.; Sadus, Richard J.
Dynamic and coordinating domain motions in the active subunits of the F-1-ATPase molecular motor
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 1764:1553-1560, OCT 2006
F-1-ATPase is a rotary molecular motor crucial for various cellular functions. In F-1-ATPase, the rotation of the gamma delta epsilon subunits against the hexameric alpha(3)beta(3) subunits is highly coordinative, driven by ATP hydrolysis and structural changes at three beta subunits. However, the dynamical and coordinating structural transitions in the beta subunits are not fully understood at the molecular level. Here we examine structural transitions and domain motions in the active subunits of F-1-ATPase via dynamical domain analysis of the alpha(3)beta(3)gamma delta epsilon complex.-The domain movement and hinge axes and bending residues have been identified and determined for various conformational changes of the beta-subunits. P-loop and the ATP-binding pocket are for the first time found to play essential mechanical functions additional to the catalytic roles. The cooperative conformational changes pertaining to the rotary mechanism of F-1-ATPase appears to be more complex than Boyer's 'bi-site' activity. These findings provide unique molecular insights into dynamic and cooperative domain motions in F-1-ATPase. (c) 2006 Elsevier B.V. All rights reserved.
