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Structural features of the ε subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy

Nature Structural Biology volume 2, pages 961–967 (1995)Cite this article

Abstract

The tertiary fold of the ε subunit of the Escherichia coli F1F0 ATPsynthase (ECF1F0) has been determined by two- and three-dimensional heteronuclear (13C, 15N) NMR spectroscopy. The ε subunit exhibits a distinct two domain structure, with the N-terminal 84 residues of the protein forming a 10-stranded β-structure, and with the C-terminal 48 amino acids arranged as two α-helices running antiparallel to one another (two helix hairpin). The β-domain folds as a β-sandwich with a hydrophobic interior between the two layers of the sandwich. The C-terminal two-helix hairpin folds back to the N-terminal domain and interacts with one side of the β-domain. The arrangement of the ε subunit in the intact F1F0 ATP synthase involves interaction of the two helix hairpin with the F1 part, and binding of the open side of the β-sandwich to the c subunits of the membrane-embedded F0 part.

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Authors and Affiliations

  1. Institute of Molecular Biology, University of Oregon, Eugene, Oregon, 97401, USA

    Stephan Wilkens, Frederick W. Dahlquist & Roderick A. Capaldi

  2. Department of Biochemistry and Molecular Biology and Department of Chemistry, University of British Columbia, Vancouver, British Columbia, V6T1Z3, Canada

    Lawrence P. McIntosh & Logan W. Donaldson

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  1. Stephan Wilkens
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  2. Frederick W. Dahlquist
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  3. Lawrence P. McIntosh
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  4. Logan W. Donaldson
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  5. Roderick A. Capaldi
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Wilkens, S., Dahlquist, F., McIntosh, L. et al. Structural features of the ε subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy. Nat Struct Mol Biol 2, 961–967 (1995). https://doi.org/10.1038/nsb1195-961

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