Structure of the cytosolic part of the subunit b-dimer of Escherichia coli F0F1-ATP synthase

Tassilo Hornung, Oleg A. Volkov, Tarek M.A. Zaida, Sabine Delannoy, John G. Wise, Pia D. Vogel

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


The structure of the external stalk and its function in the catalytic mechanism of the F0F1-ATP synthase remains one of the important questions in bioenergetics. The external stalk has been proposed to be either a rigid stator that binds F1 or an elastic structural element that transmits energy from the small rotational steps of subunits c to the F1 sector during catalysis. We employed proteomics, sequence-based structure prediction, molecular modeling, and electron spin resonance spectroscopy using site-directed spin labeling to understand the structure and interfacial packing of the Escherichia coli b-subunit homodimer external stalk. Comparisons of bacterial, cyanobacterial, and plant b-subunits demonstrated little sequence similarity. Supersecondary structure predictions, however, show that all compared b-sequences have extensive heptad repeats, suggesting that the proteins all are capable of packing as left-handed coiled-coils. Molecular modeling subsequently indicated that b2 from the E. coli ATP synthase could pack into stable left-handed coiled-coils. Thirty-eight substitutions to cysteine in soluble b-constructs allowed the introduction of spin labels and the determination of intersubunit distances by ESR. These distances correlated well with molecular modeling results and strongly suggest that the E. coli subunit b-dimer can stably exist as a left-handed coiled-coil.

Original languageEnglish (US)
Pages (from-to)5053-5064
Number of pages12
JournalBiophysical journal
Issue number12
StatePublished - Jun 15 2008

ASJC Scopus subject areas

  • Biophysics


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