A dynamic analysis of the rotation mechanism for conformational change in F(1)-ATPase.

TitleA dynamic analysis of the rotation mechanism for conformational change in F(1)-ATPase.
Publication TypeJournal Article
Year of Publication2002
AuthorsMa, J, Flynn, TC, Cui, Q, Leslie, AGW, Walker, JE, Karplus, M
JournalStructure
Volume10
Issue7
Pagination921-31
Date Published2002 Jul
ISSN0969-2126
KeywordsCrystallography, X-Ray, Models, Molecular, Protein Conformation, Protein Subunits, Proton-Translocating ATPases
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 (120 degrees 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 120 degrees rotation cycles of F(1)-ATPase.

DOI10.1016/s0969-2126(02)00789-x
Alternate JournalStructure
Citation Key10.1016/s0969-2126(02)00789-x
PubMed ID12121647