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The structure of a plant photosystem I supercomplex at 3.4 Å resolution

Abstract

All higher organisms on Earth receive energy directly or indirectly from oxygenic photosynthesis performed by plants, green algae and cyanobacteria. Photosystem I (PSI) is a supercomplex of a reaction centre and light-harvesting complexes. It generates the most negative redox potential in nature, and thus largely determines the global amount of enthalpy in living systems. We report the structure of plant PSI at 3.4 Å resolution, revealing 17 protein subunits. PsaN was identified in the luminal side of the supercomplex, and most of the amino acids in the reaction centre were traced. The crystal structure of PSI provides a picture at near atomic detail of 11 out of 12 protein subunits of the reaction centre. At this level, 168 chlorophylls (65 assigned with orientations for Qx and Qy transition dipole moments), 2 phylloquinones, 3 Fe4S4 clusters and 5 carotenoids are described. This structural information extends the understanding of the most efficient nano-photochemical machine in nature.

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Figure 1: The structural model of plant photosystem I at 3.4 Å resolution.
Figure 2: Position of β-carotenes in relation to the ETC.
Figure 3: The position of PsaN in relation to Lhca2 and Lhca3, and the unique fold of Lhca3.
Figure 4: Model for PSI–LHCII interactions.

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Acknowledgements

We thank the ESRF for synchrotron beam time, and staff scientists of the ID 14, ID 29 and ID 23 station clusters for their assistance. We also thank F. Frolow and J. Hirsh for valuable guidance and advice in crystallography. This work was supported by The Israel Science Foundation.

Atomic coordinates and structure factor files were deposited in the Protein Data Bank under accession number 2O01.

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Correspondence to Nathan Nelson.

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This file contains Supplementary Notes, Supplementary Tables S1-S2, Supplementary Figures S1-S3 with Legends and additional references. (PDF 10976 kb)

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Amunts, A., Drory, O. & Nelson, N. The structure of a plant photosystem I supercomplex at 3.4 Å resolution. Nature 447, 58–63 (2007). https://doi.org/10.1038/nature05687

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