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The structure of the central stalk in bovine F1-ATPase at 2.4 Å resolution

Nature Structural Biology volume 7, pages 1055–1061 (2000)Cite this article

Abstract

The central stalk in ATP synthase, made of γ, δ and ɛ subunits in the mitochondrial enzyme, is the key rotary element in the enzyme's catalytic mechanism. The γ subunit penetrates the catalytic (αβ)3 domain and protrudes beneath it, interacting with a ring of c subunits in the membrane that drives rotation of the stalk during ATP synthesis. In other crystals of F1-ATPase, the protrusion was disordered, but with crystals of F1-ATPase inhibited with dicyclohexylcarbodiimide, the complete structure was revealed. The δ and ɛ subunits interact with a Rossmann fold in the γ subunit, forming a foot. In ATP synthase, this foot interacts with the c-ring and couples the transmembrane proton motive force to catalysis in the (αβ)3 domain.

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Figure 1: Space filling model of bovine F1-ATPase.
Figure 2: The structure of the central stalk.
Figure 3: Stereo view of the electron density for strands 3, 2, 1, 4 and 5 (from left to right) of the γ subunit.
Figure 4: The structures of the individual stalk subunits.
Figure 5: Interaction of γArg 75 with residues in the α and β subunits to form part of the catalytic 'catch'.
Figure 6: The DCCD binding pocket in bovine F1-ATPase.

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Acknowledgements

We thank the staff at the SRS, Daresbury, UK, for their support during data collection, and D. Stock and J. Li for their help during CNS refinement. C.G. is supported by a Medical Research Council PhD studentship.

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Authors and Affiliations

  1. The Medical Research Council Dunn Human Nutrition Unit , Hills Road, Cambridge, CB2 2XY, UK

    Clyde Gibbons, Martin G. Montgomery & John E. Walker

  2. The Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK

    Andrew G. W. Leslie

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  1. Clyde Gibbons
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Correspondence to Andrew G. W. Leslie or John E. Walker.

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Gibbons, C., Montgomery, M., Leslie, A. et al. The structure of the central stalk in bovine F1-ATPase at 2.4 Å resolution. Nat Struct Mol Biol 7, 1055–1061 (2000). https://doi.org/10.1038/80981

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