%0 Journal Article %1 hlwoodcock:P.2002 %A Ma, J. P. %A Flynn, T. C. %A Cui, Q. %A Leslie, A. G. W. %A Walker, J. E. %A Karplus, M. %D 2002 %J Structure %K groel mechanism catalysis resolution simulation atpase rotary synthase molecular-dynamics f1- bibtex-import beta-subunit atp allosteric program %N 7 %P 921--931 %T A dynamic analysis of the rotation mechanism for conformational change in f-1-atpase %V 10 %X Molecular dynamics trajectories for the bovine mitochondrial F- 1-ATPase are used to demonstrate the motions and interactions that take place during the elementary (120degrees rotation) step of the gamma subunit. The results show how rotation of the gamma subunit induces the observed structural changes in the catalytic beta subunits. Both steric and electrostatic interactions contribute. An "ionic track" of Arg and Lys residues on the protruding portion of the gamma subunit plays a role in guiding the motions of the beta subunits. Experimental data for mutants of the DELSEED motif and the hinge region are interpreted on the basis of the molecular dynamics results. The trajectory provides a unified dynamic description of the coupled subunit motions involved in the 120degrees rotation cycles of F-1-ATPase.

@article{hlwoodcock:P.2002, abstract = {Molecular dynamics trajectories for the bovine mitochondrial F- 1-ATPase are used to demonstrate the motions and interactions that take place during the elementary (120degrees rotation) step of the gamma subunit. The results show how rotation of the gamma subunit induces the observed structural changes in the catalytic beta subunits. Both steric and electrostatic interactions contribute. An "ionic track" of Arg and Lys residues on the protruding portion of the gamma subunit plays a role in guiding the motions of the beta subunits. Experimental data for mutants of the DELSEED motif and the hinge region are interpreted on the basis of the molecular dynamics results. The trajectory provides a unified dynamic description of the coupled subunit motions involved in the 120degrees rotation cycles of F-1-ATPase.}, added-at = {2006-06-16T05:03:46.000+0200}, author = {Ma, J. P. and Flynn, T. C. and Cui, Q. and Leslie, A. G. W. and Walker, J. E. and Karplus, M.}, biburl = {https://www.bibsonomy.org/bibtex/2f3905b13d2013b64848f19b0250d6b5f/hlwoodcock}, citeulike-article-id = {569408}, comment = {569LF STRUCTURE}, interhash = {aacd59bd9fd4e62b520081f8c7f42204}, intrahash = {f3905b13d2013b64848f19b0250d6b5f}, journal = {Structure}, keywords = {groel mechanism catalysis resolution simulation atpase rotary synthase molecular-dynamics f1- bibtex-import beta-subunit atp allosteric program}, number = 7, pages = {921--931}, priority = {2}, timestamp = {2006-06-16T05:03:46.000+0200}, title = {A dynamic analysis of the rotation mechanism for conformational change in f-1-atpase}, volume = 10, year = 2002 }