The Unbinding of ATP from F1-ATPase

@article{citeulike:2066884, abstract = {Using molecular dynamics, we study the unbinding of ATP in F1-ATPase from its tight binding state to its weak binding state. The calculations are made feasible through use of interpolated atomic structures from Wang and Oster [Nature 1998, 396: 279-282]. These structures are applied to atoms distant from the catalytic site. The forces from these distant atoms gradually drive a large primary region through a series of sixteen equilibrated steps that trace the hinge bending conformational change in the {beta}-subunit that drives rotation of{gamma} -subunit. As the rotation progresses, we find a sequential weakening and breaking of the hydrogen bonds between the ATP molecule and the{alpha} - and {beta}-subunits of the ATPase. This finding agrees with the "binding-zipper" model [Oster and Wang, Biochim. Biophys. Acta 2000, 1458: 482-510.] In this model, the progressive formation of the hydrogen bonds is the energy source driving the rotation of the{gamma} -shaft during hydrolysis. Conversely, the corresponding sequential breaking of these bonds is driven by rotation of the shaft during ATP synthesis. Our results for the energetics during rotation suggest that the nucleotide's coordination with Mg2+ during binding and release is necessary to account for the observed high efficiency of the motor.}, author = {Antes, Iris and Chandler, David and Wang, Hongyun and Oster, George }, citeulike-article-id = {2066884}, journal = {Biophys. J.}, keywords = {clip, f1-atpase, fullatom, ligand, md}, month = {August}, number = {2}, pages = {695--706}, posted-at = {2007-12-06 13:25:44}, priority = {2}, title = {The Unbinding of ATP from F1-ATPase}, url = {http://www.biophysj.org/cgi/content/abstract/85/2/695}, volume = {85}, year = {2003} }

TY - JOUR ID - citeulike:2066884 L3 - citeulike-article-id:2066884 TI - The Unbinding of ATP from F1-ATPase JF - Biophys. J. VL - 85 IS - 2 SP - 695 EP - 706 N2 - Using molecular dynamics, we study the unbinding of ATP in F1-ATPase from its tight binding state to its weak binding state. The calculations are made feasible through use of interpolated atomic structures from Wang and Oster [Nature 1998, 396: 279-282]. These structures are applied to atoms distant from the catalytic site. The forces from these distant atoms gradually drive a large primary region through a series of sixteen equilibrated steps that trace the hinge bending conformational change in the {beta}-subunit that drives rotation of{gamma} -subunit. As the rotation progresses, we find a sequential weakening and breaking of the hydrogen bonds between the ATP molecule and the{alpha} - and {beta}-subunits of the ATPase. This finding agrees with the "binding-zipper" model [Oster and Wang, Biochim. Biophys. Acta 2000, 1458: 482-510.] In this model, the progressive formation of the hydrogen bonds is the energy source driving the rotation of the{gamma} -shaft during hydrolysis. Conversely, the corresponding sequential breaking of these bonds is driven by rotation of the shaft during ATP synthesis. Our results for the energetics during rotation suggest that the nucleotide's coordination with Mg2+ during binding and release is necessary to account for the observed high efficiency of the motor. KW - clip KW - f1-atpase KW - fullatom KW - ligand KW - md AU - Antes, Iris AU - Chandler, David AU - Wang, Hongyun AU - Oster, George PY - 2003/08/01/ UR - http://www.biophysj.org/cgi/content/abstract/85/2/695 ER -