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Structural changes linked to proton translocation by subunit c of the ATP synthase

Author

Listed:
  • Vinit K. Rastogi

    (Albert Einstein College of Medicine)

  • Mark E. Girvin

    (Albert Einstein College of Medicine)

Abstract

F1FO ATP synthases use a transmembrane proton gradient to drive the synthesis of cellular ATP. The structure of the cytosolic F1 portion of the enzyme and the basic mechanism of ATP hydrolysis by F1 are now well established, but how proton translocation through the transmembrane FO portion drives these catalytic changes is less clear. Here we describe the structural changes in the proton-translocating FO subunit c that are induced by deprotonating the specific aspartic acid involved in proton transport. Conformational changes between the protonated and deprotonated forms of subunit c provide the structural basis for an explicit mechanism to explain coupling of proton translocation by FO to the rotation of subunits within the core of F1. Rotation of these subunits within F1 causes the catalytic conformational changes in the active sites of F1 that result in ATP synthesis.

Suggested Citation

  • Vinit K. Rastogi & Mark E. Girvin, 1999. "Structural changes linked to proton translocation by subunit c of the ATP synthase," Nature, Nature, vol. 402(6759), pages 263-268, November.
    • Handle: RePEc:nat:nature:v:402:y:1999:i:6759:d:10.1038_46224
    DOI: 10.1038/46224
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    Cited by:

    1. Jun-ichi Kishikawa & Yui Nishida & Atsuki Nakano & Takayuki Kato & Kaoru Mitsuoka & Kei-ichi Okazaki & Ken Yokoyama, 2024. "Rotary mechanism of the prokaryotic Vo motor driven by proton motive force," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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