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

  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},
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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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.
The role of the DELSEED motif of the beta subunit in rotation of F1-ATPase.
It is concluded that side chains of the DELSEED motif of the beta subunit do not have a direct role in torque generation.
The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin.
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Molecular architecture of the rotary motor in ATP synthase.
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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.
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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