SGD Paper 
Kabaleeswaran V, et al. (2009) Asymmetric structure of the yeast f1 ATPase in the absence of bound nucleotides. J Biol Chem 284(16):10546-51
Abstract: The crystal structure of nucleotide free yeast F(1)-ATPase has been determined at a resolution of 3.6A. 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 in spite of 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 apo-enzyme, suggesting that the beta(DP) subunit is responsible for unisite catalytic activity.
| Status: Published | Type: Journal Article | PubMed ID: 19233840 |
Topics addressed in this paper
Number of different genes curated to this paper: 5
- To find other papers on a gene and topic, click on the colored ball in the appropriate box.
- displays other papers with information about that topic for that gene.
- displays other papers in SGD that are associated with that topic.
The topic is addressed in these papers but does not describe a specific gene or chromosomal feature.
- To go to the Locus page for a gene, click on the gene name.
