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Two-dimensional structure of plant photosystem II at 8-Å resolution

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Abstract

The photosystem II complex, which is the most abundant membrane protein in chloroplasts, comprises the light-harvesting complex II and a reaction-centre core. The reaction centre uses the solar energy collected by the light-harvesting complex II to withdraw electrons from water, releasing oxygen into the atmosphere. It thus generates an electrochemical potential, providing the energy for carbon dioxide fixation and the synthesis of organic molecules, which make up the bulk of the biosphere1. The structure of the light-harvesting complex II has been determined at 3.4-Å resolution by electron crystallography2, but the high-resolution structure of the photosystem II reaction centre and other core components remained unknown. We have grown well-ordered two-dimensional crystals of a sub-core complex containing the reaction centre from spinach thylakoid membranes and used electron crystallography to obtain a projection map of its structure at 8-Å resolution. The features reveal the likely location of the key components that are active in electron transport, and suggest a structural homology and evolutionary links, not only with the purple bacterial reaction centre but also with the reaction centre of photosystem I.

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Figure 1: Fourier transform of an untilted image of a two-dimensional crystal of PSII.
Figure 2: Projection map of PSII from spinach at 8-Å resolution, calculated from merged amplitudes and phases.
Figure 3: Comparison of the two-dimensional projected structures of the bacterial reaction centre, cyanobacterial PSI and plant PSII at 8-Å resolution.
Figure 4: Comparison of the two-dimensional projected structures of the bacterial reaction centre, cyanobacterial PSI and plant PSII at 8-Å re.
Figure 5: Comparison of the two-dimensional projected structures of the bacterial reaction centre, cyanobacterial PSI and plant PSII at 8-Å re.
Figure 6: Comparison of the two-dimensional projected structures of the bacterial reaction centre, cyanobacterial PSI and plant PSII at 8-Å re.
Figure 7: Comparison of the two-dimensional projected structures of the bacterial reaction centre, cyanobacterial PSI and plant PSII at 8-Å re.
Figure 8: Comparison of the two-dimensional projected structures of the bacterial reaction centre, cyanobacterial PSI and plant PSII at 8-Å re.
Figure 9: Superposition of the outline of the 8-Å projection map of the sub-core complex (red) with the PSII supercore complex dimer, as deter.

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Acknowledgements

We thank G. Friso for her involvement in the project, W. Schubert for supplying PSI data, and E. Orlova for advice on alignment by cross-correlation. This work was supported by the Biotechnology and Biological Sciences Research Council (J.B.) and by a fellowship to K.-H.R. from the Boehringer Ingelheim Fonds.

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  1. Kyong-Hi Rhee & Werner Kühlbrandt

    Present address: Max-Planck-Institut für Biophysik, Heinrich-Hoffmann-Strasse 7, D-60528, Frankfurt, Germany

Authors and Affiliations

  1. European Molecular Biology Laboratory, Meyerhofstrasse 1, Heidelberg, D-69117, Germany

    Kyong-Hi Rhee & Werner Kühlbrandt

  2. Department of Biochemistry, Wolfson Laboratories, Imperial College of Science, Technology and Medicine, London, SW7 2AY, UK

    Ed P. Morris, Daniela Zheleva, Ben Hankamer & James Barber

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  1. Kyong-Hi Rhee
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  2. Ed P. Morris
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Correspondence to Werner Kühlbrandt.

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Rhee, KH., Morris, E., Zheleva, D. et al. Two-dimensional structure of plant photosystem II at 8-Å resolution. Nature 389, 522–526 (1997). https://doi.org/10.1038/39103

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