Ontology highlight
ABSTRACT:
SUBMITTER: Kabaleeswaran V
PROVIDER: S-EPMC2667741 | biostudies-literature | 2009 Apr
REPOSITORIES: biostudies-literature
The Journal of biological chemistry 20090220 16
The crystal structure of nucleotide-free yeast F(1) ATPase has been determined at a resolution of 3.6 A. The overall structure is very similar to that of the ground state enzyme. In particular, the beta(DP) and beta(TP) subunits both adopt the closed conformation found in the ground state structure despite the absence of bound nucleotides. This implies that interactions between the gamma and beta subunits are as important as nucleotide occupancy in determining the conformational state of the bet ...[more]