Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria

@article{Abrahams1994StructureA2,
  title={Structure at 2.8 {\^A} resolution of F1-ATPase from bovine heart mitochondria},
  author={J. Abrahams and A. Leslie and R. Lutter and John E. Walker},
  journal={Nature},
  year={1994},
  volume={370},
  pages={621-628}
}
In the crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 Å resolution, the three catalytic β-subunits differ in conformation and in the bound nucleotide. The structure supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant. Interconversion of the states may be achieved by rotation of the α3β3 subassembly relative to an α-helical domain of the γ-subunit. 
Structure of Bovine Mitochondrial F1-ATPase with Nucleotide Bound to All Three Catalytic Sites Implications for the Mechanism of Rotary Catalysis
TLDR
A catalytic scheme for hydrolysis (and synthesis) at physiological rates and a mechanism for the ATP-driven rotation of the gamma subunit are proposed based on the crystal structures of the bovine enzyme. Expand
Structural model of F1-ATPase and the implications for rotary catalysis.
  • A. Leslie, J. Walker
  • Chemistry, Medicine
  • Philosophical transactions of the Royal Society of London. Series B, Biological sciences
  • 2000
TLDR
The crystal structure of bovine mitochondrial F1-ATPase is described, which suggests that catalysis is accompanied by a physical rotation of the centrally placed gamma-subunit relative to the approximately spherical alpha3beta3 subassembly. Expand
The structure of the central stalk in bovine F1-ATPase at 2.4 Å resolution
TLDR
The central stalk in ATP synthase is made of γ, δ and ɛ subunits in the mitochondrial enzyme, and with crystals of F1-ATPase inhibited with dicyclohexylcarbodiimide, the complete structure was revealed. Expand
Ground State Structure of F1-ATPase from Bovine Heart Mitochondria at 1.9 Å Resolution*
TLDR
The structure with bound azide represents the ADP inhibited state of the enzyme, and the new structure represents a ground state intermediate in the active catalytic cycle of ATP hydrolysis. Expand
The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis.
TLDR
In the structure of the rat liver F1-ATPase, determined to 2.8-A resolution in the presence of physiological concentrations of nucleotides, all three beta subunits contain bound nucleotide and adopt similar conformations, which suggests a mechanism of ATP synthesis/hydrolysis in which configurations of the enzyme with three bound nucleotide play an essential role. Expand
The structure of bovine F1-ATPase in complex with its regulatory protein IF1
TLDR
In mitochondria, the hydrolytic activity of ATP synthase is prevented by an inhibitor protein, IF1, which implies that the inhibited state represents a pre-hydrolysis step on the catalytic pathway of the enzyme. Expand
Asymmetric Structure of the Yeast F1 ATPase in the Absence of Bound Nucleotides*
TLDR
The crystal structure of nucleotide-free yeast F1 ATPase has been determined and the adenine-binding pocket of the βTP subunits is disrupted in the apoenzyme, suggesting that the βDP subunit is responsible for unisite catalytic activity. Expand
The Structure of the Chloroplast F1-ATPase at 3.2 Å Resolution*
TLDR
The structure probably represents an inactive latent state of the ATPase, which is unique to chloroplast and cyanobacterial enzymes, and probably represents the C-terminal domain of the γ-subunit. Expand
The ATP synthase--a splendid molecular machine.
  • P. Boyer
  • Chemistry, Medicine
  • Annual review of biochemistry
  • 1997
An X-ray structure of the F1 portion of the mitochondrial ATP synthase shows asymmetry and differences in nucleotide binding of the catalytic beta subunits that support the binding change mechanismExpand
Structure of the ATP synthase catalytic complex (F1) from Escherichia coli in an auto-inhibited conformation
TLDR
The crystal structure of the ATP synthase catalytic complex (F1) from Escherichia coli described here reveals the structural basis for autoinhibition by one of its rotary stalk subunits, and adopts a heretofore unknown, highly extended conformation that inserts deeply into the central cavity of the enzyme. Expand
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