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The dynamic stator stalk of rotary ATPases

Author

Listed:
  • Alastair G. Stewart

    (The Victor Chang Cardiac Research Institute
    Faculty of Medicine, University of New South Wales)

  • Lawrence K. Lee

    (The Victor Chang Cardiac Research Institute
    Faculty of Medicine, University of New South Wales)

  • Mhairi Donohoe

    (The Victor Chang Cardiac Research Institute
    Present address: National Neuroscience Facility, Melbourne, Australia.)

  • Jessica J. Chaston

    (The Victor Chang Cardiac Research Institute)

  • Daniela Stock

    (The Victor Chang Cardiac Research Institute
    Faculty of Medicine, University of New South Wales)

Abstract

Rotary ATPases couple ATP hydrolysis/synthesis with proton translocation across biological membranes and so are central components of the biological energy conversion machinery. Their peripheral stalks are essential components that counteract torque generated by rotation of the central stalk during ATP synthesis or hydrolysis. Here we present a 2.25-Å resolution crystal structure of the peripheral stalk from Thermus thermophilus A-type ATPase/synthase. We identify bending and twisting motions inherent within the structure that accommodate and complement a radial wobbling of the ATPase headgroup as it progresses through its catalytic cycles, while still retaining azimuthal stiffness necessary to counteract rotation of the central stalk. The conformational freedom of the peripheral stalk is dictated by its unusual right-handed coiled-coil architecture, which is in principle conserved across all rotary ATPases. In context of the intact enzyme, the dynamics of the peripheral stalks provides a potential mechanism for cooperativity between distant parts of rotary ATPases.

Suggested Citation

  • Alastair G. Stewart & Lawrence K. Lee & Mhairi Donohoe & Jessica J. Chaston & Daniela Stock, 2012. "The dynamic stator stalk of rotary ATPases," Nature Communications, Nature, vol. 3(1), pages 1-8, January.
    • Handle: RePEc:nat:natcom:v:3:y:2012:i:1:d:10.1038_ncomms1693
    DOI: 10.1038/ncomms1693
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