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Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria

Nature volume 370, pages 621–628 (1994)Cite this article

Abstract

In the crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 Å resolution, the three catalytic β-subunits differ in conformation and in the bound nucleotide. The structure supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant. Interconversion of the states may be achieved by rotation of the α3β3 subassembly relative to an α-helical domain of the γ-subunit.

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Author notes

  1. René Lutter

    Present address: Academic Medical Centre, Department of Pulmonology, University of Amsterdam, Meibergdreef 9, 1105 AZ, Amsterdam, The Netherlands

Authors and Affiliations

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

    Jan Pieter Abrahams, Andrew G. W. Leslie, René Lutter & John E. Walker

Authors
  1. Jan Pieter Abrahams
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  2. Andrew G. W. Leslie
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  3. René Lutter
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  4. John E. Walker
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Abrahams, J., Leslie, A., Lutter, R. et al. Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria. Nature 370, 621–628 (1994). https://doi.org/10.1038/370621a0

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