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

Nature volume 389, pages 522–526 (1997)Cite this article

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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References

  1. Barber, J. & Andersson, B. Revealing the blueprint of photosynthesis. Nature 370, 31–34 (1994).

    Article  ADS  CAS  Google Scholar 

  2. Kühlbrandt, W., Wang, D. N. & Fujiyoshi, Y. Atomic model of plant light-harvesting complex by electron crystallography. Nature 367, 614–621 (1994).

    Article  ADS  Google Scholar 

  3. Nanba, O. & Satoh, K. Isolation of a photosystem II reaction center consisting of D-1 and D-2 polypeptides and cytochrome b-559. Proc. Natl Acad. Sci. USA 84, 109–112 (1987).

    Article  ADS  CAS  Google Scholar 

  4. Barber, J. et al. Characterisation of a PS II reaction centre isolated from the chloroplasts of Pisum sativum. FEBS Lett. 220, 67–73 (1987).

    Article  CAS  Google Scholar 

  5. Jansson, S. The light-harvesting chlorophyll a/b -binding proteins. Biochim. Biophys. Acta 1184, 1–19 (1994).

    Article  CAS  Google Scholar 

  6. Nakazato, K. et al. Two-dimensional crystallization and cryo-electron microscopy of photosystem II. J. Mol. Biol. 257, 225–232 (1996).

    Article  CAS  Google Scholar 

  7. Michel, H. et al. The ‘light’ and ‘medium’ subunits of the photosynthetic reaction centre from Rhodopseudomonas viridis : isolation of the genes, nucleotide and amino acid sequence. EMBO J. 5, 1149–1158 (1986).

    Article  CAS  Google Scholar 

  8. Krauss, N. et al. Photosystem I at 4 Å resolution represents the first structural model of a joint photosynthetic reaction centre and core antenna system. Nature Struct. Biol. 3, 965–973 (1996).

    Article  CAS  Google Scholar 

  9. Vermaas, W. F. J. Evolution of heliobacteria: implications for photosynthetic reaction center complexes. Photosynth. Res. 41, 285–294 (1994).

    Article  CAS  Google Scholar 

  10. Rutherford, A. W. & Nitschke, W. in Origin and Evolution of Biological Energy Conversion, (ed. Baltscheffsky, H.) 143–174 (VCH, New York, (1996)).

    Google Scholar 

  11. Fromme, P. et al. Structure of Photosystem I at 4.5 Å resolution: A short review including evolutionary aspects. Biochim. Biophys. Acta. 1275, 76–83 (1996).

    Article  Google Scholar 

  12. Boekema, E. J. et al. Supramolecular structure of the photosystem II complex from green plants and cyanobacteria. Proc. Natl Acad. Sci. USA 92, 175–179 (1995).

    Article  ADS  CAS  Google Scholar 

  13. Wang, D. N. & Kühlbrandt, W. High-resolution electron crystallography of light-harvesting chlorophyll a/b -protein complex in three different media. J. Mol. Biol. 217, 691–699 (1991).

    Article  CAS  Google Scholar 

  14. Henderson, R., Baldwin, J. M., Downing, K. H., Lepault, J. & Zemlin, F. Structure of purple membrane from Halobacterium halobium : recording, measurement and evaluation of electron micrographs at 3.5 Å resolution. Ultramicroscopy 19, 147–178 (1986).

    Article  CAS  Google Scholar 

  15. Henderson, R. et al. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213, 899–929 (1990).

    Article  CAS  Google Scholar 

  16. Frank, J., Shimkin, B. & Dowse, H. SPIDER-A modular software system for electron image processing. Ultramicroscopy 6, 343–358 (1981).

    Article  Google Scholar 

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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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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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