Conformational dynamics of the F1-ATPase beta-subunit: a molecular dynamics study.

ABSTRACT: According to the different nucleotide occupancies of the F(1)-ATPase beta-subunits and due to the asymmetry imposed through the central gamma-subunit, the beta-subunit adopts different conformations in the crystal structures. Recently, a spontaneous and nucleotide-independent closure of the open beta-subunit upon rotation of the gamma-subunit has been proposed. To address the question whether this closure is dictated by interactions to neighbored subunits or whether the open beta-subunit behaves like a prestressed "spring," we report multinanosecond molecular dynamics simulations of the isolated beta-subunit with different start conformations and different nucleotide occupancies. We have observed a fast, spontaneous closure motion of the open beta(E)-subunit, consistent with the available

SUBMITTER: Bockmann RA 

PROVIDER: S-EPMC1303325 | biostudies-literature | 2003 Sep

REPOSITORIES: biostudies-literature