Structure of bovine mitochondrial F(1)-ATPase inhibited by Mg(2+) ADP and aluminium fluoride.

  title={Structure of bovine mitochondrial F(1)-ATPase inhibited by Mg(2+) ADP and aluminium fluoride.},
  author={Kerstin Braig and Robert Ian Menz and Martin G. Montgomery and Andrew G W Leslie and John E. Walker},
  volume={8 6},
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.
How azide inhibits ATP hydrolysis by the F-ATPases.
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
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 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.
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.
Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review)
The energetics associated with two different models of the reaction steps, analysed using molecular dynamics calculations, show that three-nucleotide intermediates do not occur in configurations with an open β subunit; instead, they are stabilized by completing a jaw-like motion that closes the β sub unit around the nucleotide.
ATP Synthesis by Oxidative Phosphorylation.
  • S. Vik
  • Biology, Chemistry
    EcoSal Plus
  • 2007
The F1F0-ATP synthase (EC is a remarkable enzyme that functions as a rotary motor. It is found in the inner membranes of Escherichia coli and is responsible for the synthesis of ATP in
Mitochondrial ATP synthase catalytic mechanism: a novel visual comparative structural approach emphasizes pivotal roles for Mg²⁺ and P-loop residues in making ATP.
The results of these studies reported here show that the absence of Mg(2+) results in migration of inorganic phosphate from βA158 to a more medial position in the P-loop binding pocket, thereby disrupting essential placement and orientation of the P(i) needed to form the transition state structure and therefore MgATP.


Inhibition of H+-transporting ATPase by formation of a tight nucleoside diphosphate-fluoroaluminate complex at the catalytic site.
  • J. Lunardi, A. Dupuis, P. Vignais
  • Chemistry, Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1988
AIF4- is postulated to mimic the phosphate group of ATP and form an abortive complex with ADP at the active site(s) of F1-type ATPase, suggesting that aluminum acts through a tetrahedral complex.
Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria
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.
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
Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis.
AlF4- complexes formed by the G protein Gi alpha 1 demonstrate specific roles in transition-state stabilization for two highly conserved residues, suggesting a mechanism that may promote release of the beta gamma subunit complex when the alpha subunit is activated by GTP.
Direct observation of the rotation of F1-ATPase
It is shown that a single molecule of F1-ATPase acts as a rotary motor, the smallest known, by direct observation of its motion by attaching a fluorescent actin filament to the γ-subunit as a marker, which enabled us to observe this motion directly.
The role of beta-Arg-182, an essential catalytic site residue in Escherichia coli F1-ATPase.
It was found that beta-Arg-182 interacts with the gamma-phosphate of MgATP, particularly at catalytic sites 1 and 2, and resembles that of another positively charged residue in the catalytic site, the conserved lysine of the Walker A motif, beta-Lys-155.
GTPase mechanism of Gproteins from the 1.7-Å crystal structure of transducin α - GDP AIF−4
ALUMINIUM fluoride (A1F−4) activates members of the hetero-trimeric G-protein (Gαβγ) family1,2 by binding to inactive Gα·GDP near the site occupied by the γ-phosphate in Gα·GTP (ref. 3). Here we
AlF3 mimics the transition state of protein phosphorylation in the crystal structure of nucleoside diphosphate kinase and MgADP.
The two x-ray structures show explicit enzyme-substrate interactions that discriminate between the ground and the transition states of the reaction and illustrate the partially dissociative geometry of the transition state of phosphoryl transfer and demonstrate the potential applications of metallofluorides for the study of kinase mechanisms.
X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-.
The three-dimensional structures of the truncated myosin head from Dictyostelium discoideum myOSin II complexed with beryllium and aluminum fluoride and magnesium ADP are reported, indicating that myos in undergoes a conformational change during hydrolysis that is not associated with the nucleotide binding pocket but rather occurs in the COOH-terminal segment of the myosIn motor domain.