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

@article{Gibbons2000TheSO,
  title={The structure of the central stalk in bovine F1-ATPase at 2.4 {\AA} resolution},
  author={Clyde Gibbons and Martin G. Montgomery and Andrew G W Leslie and John E. Walker},
  journal={Nature Structural Biology},
  year={2000},
  volume={7},
  pages={1055-1061}
}
The central stalk in ATP synthase, made of γ, δ and ɛ subunits in the mitochondrial enzyme, is the key rotary element in the enzyme's catalytic mechanism. The γ subunit penetrates the catalytic (αβ) 3 domain and protrudes beneath it, interacting with a ring of c subunits in the membrane that drives rotation of the stalk during ATP synthesis. In other crystals of F1-ATPase, the protrusion was disordered, but with crystals of F1-ATPase inhibited with dicyclohexylcarbodiimide, the complete… 
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References

SHOWING 1-10 OF 67 REFERENCES
The Role of the DELSEED Motif of the β Subunit in Rotation of F1-ATPase*
TLDR
It is concluded that side chains of the DELSEED motif of the β subunit do not have a direct role in torque generation in F1-ATPase.
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 role of the DELSEED motif of the beta subunit in rotation of F1-ATPase.
TLDR
It is concluded that side chains of the DELSEED motif of the beta subunit do not have a direct role in torque generation.
Crystal structure of the ϵ subunit of the proton-translocating ATP synthase from Escherichia coli
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.
Molecular architecture of the rotary motor in ATP synthase.
TLDR
An electron density map obtained from crystals of a subcomplex of yeast mitochondrial ATP synthase shows a ring of 10 c subunits whose extensive contact between the c ring and the stalk suggests that they may rotate as an ensemble during catalysis.
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…
Novel features in the structure of bovine ATP synthase.
The F1F0-ATP synthase from bovine heart mitochondria catalyses the synthesis of ATP from ADP and inorganic phosphate by using the energy of an electrochemical proton gradient derived from electron…
Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli.
BACKGROUND Proton-translocating ATP synthases convert the energy generated from photosynthesis or respiration into ATP. These enzymes, termed F0F1-ATPases, are structurally highly conserved. In…
Structure of bovine mitochondrial F(1)-ATPase inhibited by Mg(2+) ADP and aluminium fluoride.
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