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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