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

@article{Bowler2007GroundSS,
  title={Ground State Structure of F1-ATPase from Bovine Heart Mitochondria at 1.9 Å Resolution*},
  author={Matthew W. Bowler and Martin G. Montgomery and Andrew G W Leslie and John E. Walker},
  journal={Journal of Biological Chemistry},
  year={2007},
  volume={282},
  pages={14238 - 14242}
}
The structure of bovine F1-ATPase, crystallized in the presence of AMP-PNP and ADP, but in the absence of azide, has been determined at 1.9Å resolution. This structure has been compared with the previously described structure of bovine F1-ATPase determined at 1.95Å resolution with crystals grown under the same conditions but in the presence of azide. The two structures are extremely similar, but they differ in the nucleotides that are bound to the catalytic site in the βDP-subunit. In the… 

Figures and Tables from this paper

The structure of F1-ATPase from Saccharomyces cerevisiae inhibited by its regulatory protein IF1

TLDR
The structure of F1-ATPase from Saccharomyces cerevisiae inhibited by the yeast IF1 has been determined and provides further evidence of sequential product release, with the phosphate and the magnesium ion released before the ADP molecule.

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.

How the regulatory protein, IF1, inhibits F1-ATPase from bovine mitochondria

The structure of bovine F1-ATPase inhibited by a monomeric form of the inhibitor protein, IF1, known as I1–60His, lacking most of the dimerization region, has been determined at 2.1-Å resolution. The

The structure of the membrane extrinsic region of bovine ATP synthase

TLDR
The structure of the membrane extrinsic part of bovine ATP synthase is now complete and the linker region between the 2 domains of the OSCP appears to be flexible, enabling the stator to adjust its shape as it passes over the changing profile of the F1 domain during a catalytic cycle.

Structural evidence of a new catalytic intermediate in the pathway of ATP hydrolysis by F1–ATPase from bovine heart mitochondria

TLDR
The molecular description of the mechanism of F1–ATPase is based mainly on high-resolution structures of the enzyme from mitochondria, coupled with direct observations of rotation in bacterial enzymes, and has captured another intermediate in the catalytic cycle, which helps to define the order of substrate release.

Identification of the βTP site in the x-ray structure of F1-ATPase as the high-affinity catalytic site

  • H. MaoJ. Weber
  • Chemistry, Biology
    Proceedings of the National Academy of Sciences
  • 2007
TLDR
Taking into account the known direction of rotation, the findings establish the sequence of affinities through which each catalytic site cycles during MgATP hydrolysis as low → high → medium → low.

The affinity purification and characterization of ATP synthase complexes from mitochondria

TLDR
This property has been exploited in the development of a highly selective affinity procedure for purifying the intact F-ATP synthase complex from mitochondria in a single chromatographic step by using inhibitor proteins with a C-terminal affinity tag.

Stepwise Propagation of the ATP-induced Conformational Change of the F1-ATPase β Subunit Revealed by NMR*

TLDR
The chemical shift perturbation of backbone amide signals of the segmentally labeled β(mutant) s indicated stepwise propagation of the open/close conversion on ligand binding in the catalytic rotation of F1-ATPase.

Activation of MgADP-inactivated chloroplast F1-ATPase depends on oxyanion binding to noncatalytic sites

  • A. Malyan
  • Biology, Chemistry
    Doklady Biochemistry and Biophysics
  • 2013
TLDR
The effect of CF 1 preincubation with pyrophosphate (PP i) on stimulation of MgADPPinactivated CF 1 ATPase by sulfitee and bicarbonate oxyanions is considered.
...

References

SHOWING 1-10 OF 25 REFERENCES

How azide inhibits ATP hydrolysis by the F-ATPases.

TLDR
The structure of bovine F1-ATPase determined at 1.95-A resolution with crystals grown in the presence of ADP, 5'-adenylyl-imidodiphosphate, and azide explains the stimulatory effect of azide on ATP-sensitive potassium channels by enhancing the binding ofADP.

The structure of bovine F1‐ATPase inhibited by ADP and beryllium fluoride

TLDR
In the structure of F1‐ATPase with five bound ADP molecules (three in α‐subunits, one each in the βTP and βDP subunits), which has been determined, the conformation of αArg373 suggests that it senses the presence (or absence of the γ‐phosphate of ATP.

The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin.

TLDR
Efrapeptin appears to inhibit F1-ATPase by blocking the conversion of subunit beta E to a nucleotide binding conformation, as would be required by an enzyme mechanism involving cyclic interconversion of catalytic sites.

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

TLDR
The crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 Å resolution 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.

The structure of bovine F1-ATPase complexed with the antibiotic inhibitor aurovertin B.

TLDR
It is shown that the uncompetitive inhibitor aurovertin B binds to bovine F1 at two equivalent sites in betaTP and betaE, in a cleft between the nucleotide binding and C-terminal domains.

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.

Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase

TLDR
The shifts in position of the central stalk between two of the three copies of yeast F1 ATPase give new insight into the conformational changes that take place during rotational catalysis.