Cryo-EM studies of E. coli ATP synthase

Sobti M1, Smits C1, Wong ASW2, Ishmukhametov R3, Stock D1, Sandin S2 and Stewart AG1

  1. Victor Chang Cardiac Research Institute, Australia.
  2. Nanyang Technological University, Singapore.
  3. University of Oxford, United Kingdom.

ATP synthase is an essential biological motor that synthesizes the bulk of cellular ATP, the energy currency of the cell. Here we present our cryo-EM maps of the intact ATP synthase complex from Escherichia coli (1). Three different states that relate to rotation of the enzyme were observed, with the central stalk’s ε subunit in an extended auto inhibitory conformation in all three states. For the first time in this rotary ATPase subtype, the peripheral stalk is resolved over its entire length of the complex revealing the F1 attachment points and a coiled-coil that bifurcates toward the membrane. The molecular models also provide a framework onto which the vast array of information available on the widely studied E. coli enzyme can be mapped. References: 1. Sobti M, Smits C, Wong AS, Ishmukhametov R, Stock D, Sandin S, et al. eLIFE. 2016;5: e21598.