Cryo-EM studies of E. coli ATP synthase

Sobti M1, Smits C1, Wong ASW2, Ishmukhametov R3, Stock D1,4, Sandin S5 and Stewart AG1,4

  1. Molecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, Darlinghurst 2010, Australia.
  2. NTU Institute of Structural Biology, Nanyang Technological University, Singapore, Singapore.
  3. Department of Physics, Clarendon Laboratory, University of Oxford, Oxford OX1 3PU, UK.
  4. Faculty of Medicine, The University of New South Wales, Sydney 2052, Australia.
  5. School of Biological Sciences, Nanyang Technological University, Singapore, Singapore.

Here we present our cryo-EM maps of the intact ATP synthase complex from Escherichia coli. This essential enzyme synthesises the bulk of cellular ATP, the energy currency of the cell. The structures highlight unique features of this ATP synthase complex, such as the bifurcation of the peripheral stalk homodimer and the position of the inhibitory subunit ε. Further studies on this complex reveal a possible partially active conformation, which points to the molecular events that may inhibit this marvellous motor.