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={Jan Pieter Abrahams and Andrew G W Leslie and Ren{\'e} 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. 

Structural model of F1-ATPase and the implications for rotary catalysis.

  • A. LeslieJ. Walker
  • Chemistry
    Philosophical transactions of the Royal Society of London. Series B, Biological sciences
  • 2000
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.

The structure of the central stalk in bovine F1-ATPase at 2.4 Å resolution

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.

Ground State Structure of F1-ATPase from Bovine Heart Mitochondria at 1.9 Å Resolution*

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.

The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis.

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.

The structure of bovine F1-ATPase in complex with its regulatory protein IF1

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.

Asymmetric Structure of the Yeast F1 ATPase in the Absence of Bound Nucleotides*

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.

The Structure of the Chloroplast F1-ATPase at 3.2 Å Resolution*

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.

The ATP synthase--a splendid molecular machine.

  • P. Boyer
  • Chemistry
    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 mechanism

Structure of the ATP synthase catalytic complex (F1) from Escherichia coli in an auto-inhibited conformation

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.
...

References

SHOWING 1-10 OF 44 REFERENCES

Crystallization of F1-ATPase from bovine heart mitochondria.

Crystals of the F1-ATPase sector of the ATP synthase complex from bovine heart mitochondria have been grown from solutions containing polyethylene glycol 6000. The crystals diffract to 2.9 A

Inherent asymmetry of the structure of F1‐ATPase from bovine heart mitochondria at 6.5 A resolution.

The 3‐dimensional structure of bovine mitochondrial F1‐ATPase, the assembly which makes ATP in mitochondria, chloroplasts and bacteria, is determined to 6.5 A resolution by X‐ray crystallography.

The structure of the E. coli recA protein monomer and polymer

The crystal structure of the recA protein from Escherichia coli at 2.3-Å resolution reveals a major domain that binds ADP and probably single- and double-stranded DNA. Two smaller subdomains at the N

The 2.2 Å crystal structure of transducin-α complexed with GTPγS

The structure of activated rod transducin shows the bound GTPγS molecule occluded deep in a cleft between a domain structurally homologous to small GTPases and a helical domain unique to heterotrimeric G proteins, suggesting how an activated receptor might open this cleft to allow nucleotide exchange.

The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S.

The structure of activated rod transducin, Gt alpha, suggests how an activated receptor might open this cleft to allow nucleotide exchange; a mechanism for GTP-induced changes in effector and receptor binding surfaces; and a mechanismFor GTPase activity not evident from previous data.

Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondria.

Structural aspects of proton-pumping ATPases.

The sequence of the proteins of ATP-synthase have provided information about amino acids that are important for its function, and amino acids contributing to nucleotide binding sites have been identified, which provide the basis of models of secondary structure of membrane components that constitute the transmembrane proton channel.