Asymmetric structure of the yeast F1 ATPase in the absence of bound nucleotides.

TitleAsymmetric structure of the yeast F1 ATPase in the absence of bound nucleotides.
Publication TypeJournal Article
Year of Publication2009
AuthorsKabaleeswaran, V, Shen, H, Symersky, J, Walker, JE, Leslie, AGW, Mueller, DM
JournalJ Biol Chem
Volume284
Issue16
Pagination10546-51
Date Published2009 Apr 17
ISSN0021-9258
KeywordsAnimals, Cattle, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Nucleotides, Protein Conformation, Protein Subunits, Proton-Translocating ATPases, Saccharomyces cerevisiae Proteins
Abstract

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 beta subunits. Furthermore, this result suggests that for the mitochondrial enzyme, there is no state of nucleotide occupancy that would result in more than one of the beta subunits adopting the open conformation. The adenine-binding pocket of the beta(TP) subunit is disrupted in the apoenzyme, suggesting that the beta(DP) subunit is responsible for unisite catalytic activity.

DOI10.1074/jbc.M900544200
Alternate JournalJ. Biol. Chem.
Citation Key10.1074/jbc.M900544200
PubMed ID19233840
PubMed Central IDPMC2667741
Grant ListR01 GM066223-07 / GM / NIGMS NIH HHS / United States
R01 GM066223-06 / GM / NIGMS NIH HHS / United States
R01 GM066223 / GM / NIGMS NIH HHS / United States
R01 GM066223-05 / GM / NIGMS NIH HHS / United States
MC_U105184325 / / Medical Research Council / United Kingdom
MC_U105663150 / / Medical Research Council / United Kingdom