3FKS

Yeast F1 ATPase in the absence of bound nucleotides

Summary for 3FKS

• Entry DOI: 10.2210/pdb3fks/pdb
• Related: 1W0J 2HLD
• Descriptor: ATP synthase subunit alpha, mitochondrial, ATP synthase subunit beta, mitochondrial, ATP synthase subunit gamma, mitochondrial, ... (6 entities in total)
• Functional Keywords: atp synthase, atp phosphatase, f1f0 atpase, atp synthesis, atp-binding, cf(1), hydrogen ion transport, ion transport, membrane, mitochondrion, mitochondrion inner membrane, nucleotide-binding, phosphoprotein, transport, hydrolase
• Biological source: Saccharomyces cerevisiae (yeast); More
• Cellular location: Mitochondrion inner membrane : P07251; Mitochondrion: P00830 P38077 Q12165 P21306
• Total number of polymer chains: 27
• Total formula weight: 1120103.58

Authors

Kabaleeswaran, V.,Symersky, J.,Shen, H.,Walker, J.E.,Leslie, A.G.W.,Mueller, D.M. (deposition date: 2008-12-17, release date: 2009-03-03, Last modification date: 2023-09-06)

Primary citation

Kabaleeswaran, V.,Shen, H.,Symersky, J.,Walker, J.E.,Leslie, A.G.,Mueller, D.M.
Asymmetric structure of the yeast f1 ATPase in the absence of bound nucleotides.
J.Biol.Chem., 284:10546-10551, 2009

PubMed 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.

PubMed: 19233840
DOI: 10.1074/jbc.M900544200

Experimental method

X-RAY DIFFRACTION (3.587 Å)