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The Oligomeric Subunit c Rotor in the Fo Sector of ATP Synthase: Unresolved Questions in Our Understanding of Function

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Abstract

We have proposed a model for the oligomeric c-rotor of the Fo sector of ATP synthase and its interaction with subunit a during H+-transport driven rotation. The model is based upon the solution structure of monomeric subunit c, determined by NMR, and an extensive series of cross-linking distance constraints between c subunits and between subunits c and a. To explain the complete set of cross-linking data, we have suggested that the second transmembrane helix rotates during its interaction with subunit a in the course of the H+-translocation cycle. The H+-transport coupled rotation of this helix is proposed to drive the stepwise movement of the c-oligomeric rotor. The model is testable and provides a useful framework for addressing questions raised by other experiments.

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Authors and Affiliations

  1. Department of Biomolecular Chemistry, University of Wisconsin Medical School, 1300 University avenue, Madison, Wisconsin, 53706

    Robert H. Fillingame

  2. Department of Biomolecular Chemistry, University of Wisconsin Medical School, 1300 University avenue, Madison, Wisconsin, 53706

    Weiping Jiang & Oleg Y. Dmitriev

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  1. Robert H. Fillingame
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  2. Weiping Jiang
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  3. Oleg Y. Dmitriev
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Fillingame, R.H., Jiang, W. & Dmitriev, O.Y. The Oligomeric Subunit c Rotor in the Fo Sector of ATP Synthase: Unresolved Questions in Our Understanding of Function. J Bioenerg Biomembr 32, 433–439 (2000). https://doi.org/10.1023/A:1005604722178

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  • DOI: https://doi.org/10.1023/A:1005604722178

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