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

@article{Kabaleeswaran2006NovelFO,
  title={Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase},
  author={Venkataraman Kabaleeswaran and Neeti Puri and John E. Walker and Andrew G W Leslie and David M. Mueller},
  journal={The EMBO Journal},
  year={2006},
  volume={25}
}
The crystal structure of yeast mitochondrial F1 ATPase contains three independent copies of the complex, two of which have similar conformations while the third differs in the position of the central stalk relative to the α3β3 sub‐assembly. All three copies display very similar asymmetric features to those observed for the bovine enzyme, but the yeast F1 ATPase structures provide novel information. In particular, the active site that binds ADP in bovine F1 ATPase has an ATP analog bound and… 
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TLDR
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TLDR
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