Structure of the ATP synthase catalytic complex (F1) from Escherichia coli in an auto-inhibited conformation

@article{Cingolani2011StructureOT,
  title={Structure of the ATP synthase catalytic complex (F1) from Escherichia coli in an auto-inhibited conformation},
  author={Gino Cingolani and Thomas M. Duncan},
  journal={Nature structural \& molecular biology},
  year={2011},
  volume={18},
  pages={701 - 707}
}
ATP synthase is a membrane-bound rotary motor enzyme that is critical for cellular energy metabolism in all kingdoms of life. Despite conservation of its basic structure and function, autoinhibition by one of its rotary stalk subunits occurs in bacteria and chloroplasts but not in mitochondria. The crystal structure of the ATP synthase catalytic complex (F1) from Escherichia coli described here reveals the structural basis for this inhibition. The C-terminal domain of subunit ɛ adopts a… 

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