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Conformational changes in the Escherichia coli ATP synthase b-dimer upon binding to F1-ATPase

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Abstract

Conformational changes within the subunit b-dimer of the E. coli ATP synthase occur upon binding to the F1 sector. ESR spectra of spin-labeled b at room temperature indicated a pivotal point in the b-structure at residue 62. Spectra of frozen b ± F1 and calculated interspin distances suggested that where contact between b 2 and F1 occurs (above about residue 80), the structure of the dimer changes minimally. Between b-residues 33 and 64 inter-subunit distances in the F1-bound b-dimer were found to be too large to accommodate tightly coiled coil packing and therefore suggest a dissociation and disengagement of the dimer upon F1-binding. Mechanistic implications of this “bubble” formation in the tether domain of ATP synthase b 2 are discussed.

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Author notes

  1. Tassilo Hornung

    Present address: Biomedicine and Biotechnology, School of Life Sciences, Arizona State University, Tempe, AZ, USA

Authors and Affiliations

  1. Department of Biological Sciences, Southern Methodist University, 6501 Airline Rd., Dallas, TX, 75275, USA

    Tarek M. Zaida, Tassilo Hornung, Oleg A. Volkov, Andrea D. Hoffman, Susan J. Pandey, John G. Wise & Pia D. Vogel

Authors
  1. Tarek M. Zaida
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  2. Tassilo Hornung
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  3. Oleg A. Volkov
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  4. Andrea D. Hoffman
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  5. Susan J. Pandey
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  6. John G. Wise
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  7. Pia D. Vogel
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Corresponding author

Correspondence to Pia D. Vogel.

Additional information

This work was supported by grant from the National Science Foundation (MCB 0415713) to PDV

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Zaida, T.M., Hornung, T., Volkov, O.A. et al. Conformational changes in the Escherichia coli ATP synthase b-dimer upon binding to F1-ATPase. J Bioenerg Biomembr 40, 551–559 (2008). https://doi.org/10.1007/s10863-008-9189-z

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  • DOI: https://doi.org/10.1007/s10863-008-9189-z

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