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Structure of the γ–ɛ complex of ATP synthase

Nature Structural Biology volume 7, pages 1051–1054 (2000)Cite this article

Abstract

ATP synthases (F1Fo-ATPases) use energy released by the movement of protons down a transmembrane electrochemical gradient to drive the synthesis of ATP, the universal biological energy currency. Proton flow through Fo drives rotation of a ring of c-subunits and a complex of the γ and ɛ-subunits, causing cyclical conformational changes in F1 that are required for catalysis. The crystal structure of a large portion of F1 has been resolved. However, the structure of the central portion of the enzyme, through which conformational changes in Fo are communicated to F1, has until now remained elusive. Here we report the crystal structure of a complex of the ɛ-subunit and the central domain of the γ-subunit refined at 2.1 Å resolution. The structure reveals how rotation of these subunits causes large conformational changes in F1, and thereby provides new insights into energy coupling between Fo and F1.

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Figure 1: Structural arrangement of γ′ and ɛ-subunits from E. coli ATP synthase.
Figure 2: Schematic representation of the composite model of ATP synthase.
Figure 3: Stereo view of the 2Fo − Fc electron density map at 2.1 Å resolution, which is contoured at 1.4 σ.

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Acknowledgements

Use of the APS was supported by the US Department of Energy, Basic Energy Sciences, Office of Science. Use of the BioCARS Sector 14 was supported by the National Institutes of Health, National Center for Research Resources. This research was supported by grants from the National Health and Medical Research Foundation (M.C.J.W.), University of Western Australia Medical Research Fellowship (A.J.W.R.) and The Raine Medical Research Foundation (M.C.J.W.). Travel to the APS was funded from a grant from the Australian Nuclear Science and Technology Organization.

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  1. Crystallography Centre Department of Pharmacology, University of Western Australia and Western Australian Institute for Medical Research, Nedlands, 6907, Western Australia, Australia

    Andrew J. W. Rodgers & Matthew C. J. Wilce

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  1. Andrew J. W. Rodgers
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  2. Matthew C. J. Wilce
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Correspondence to Matthew C. J. Wilce.

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Rodgers, A., Wilce, M. Structure of the γ–ɛ complex of ATP synthase. Nat Struct Mol Biol 7, 1051–1054 (2000). https://doi.org/10.1038/80975

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