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Getting to the bottom of the F1-ATPase

Nature Structural Biology volume 7, pages 1002–1004 (2000)Cite this article

Two new crystal structures describe previously unresolved domains of the F1 sector of ATP synthase. These domains lie at the interface between the transmembrane rotary motor and the rotating subunits of the F1 domain and are crucial in coupling rotation of the two sectors to ATP synthesis.

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Figure 1: Rotary model for ATP synthase based on the subunit composition of the Escherichia coli enzyme.
Figure 2: Comparison of a, the structure of γ and δm subunit in bovine mitochondrial F1 and b, that of E. coli γ′–ɛec.

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  1. Department of Biomolecular Chemistry, University of Wisconsin Medical School, Madison, 53706, Wisconsin, USA

    Robert H. Fillingame

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Fillingame, R. Getting to the bottom of the F1-ATPase. Nat Struct Mol Biol 7, 1002–1004 (2000). https://doi.org/10.1038/80902

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