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

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

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish (US)
Pages (from-to)551-559
Number of pages9
JournalJournal of Bioenergetics and Biomembranes
Issue number6
StatePublished - Dec 2008


  • ATPase
  • B-dimer
  • Coiled coil
  • Conformational changes
  • ESR
  • External stalk
  • Spin-labeling

ASJC Scopus subject areas

  • Physiology
  • Cell Biology


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