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Crystal structure of plant photosystem I

Abstract

Oxygenic photosynthesis is the principal producer of both oxygen and organic matter on Earth. The conversion of sunlight into chemical energy is driven by two multisubunit membrane protein complexes named photosystem I and II. We determined the crystal structure of the complete photosystem I (PSI) from a higher plant (Pisum sativum var. alaska) to 4.4 Å resolution. Its intricate structure shows 12 core subunits, 4 different light-harvesting membrane proteins (LHCI) assembled in a half-moon shape on one side of the core, 45 transmembrane helices, 167 chlorophylls, 3 Fe–S clusters and 2 phylloquinones. About 20 chlorophylls are positioned in strategic locations in the cleft between LHCI and the core. This structure provides a framework for exploration not only of energy and electron transfer but also of the evolutionary forces that shaped the photosynthetic apparatus of terrestrial plants after the divergence of chloroplasts from marine cyanobacteria one billion years ago.

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Figure 1: The structural model of plant PSI at 4.4 Å represented as Cα backbone.
Figure 2: The arrangement of 167 chlorophyll molecules of plant PSI as seen from the stromal side.
Figure 3: Dimer formation between Lhca1 and Lhca4 and tight binding of Lhca1 to the reaction centre.
Figure 4: The structural model of Lhca monomers compared to LHCII.
Figure 5: Electron transfer chain and plastocyanin binding.
Figure 6: Loops altered during the evolution of plant PsaA and PsaB.

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Acknowledgements

We acknowledge the ESRF for synchrotron beam time, and staff scientists of the ID14 stations cluster for their assistance. We thank W. Kuhlbrandt for LHCII coordinates. A.B. is a recipient of a Charles Clore Foundation Ph.D. student scholarship. This work was supported by a grant from The Israel Science Foundation to N.N. and F.F.

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Correspondence to Nathan Nelson.

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Ben-Shem, A., Frolow, F. & Nelson, N. Crystal structure of plant photosystem I. Nature 426, 630–635 (2003). https://doi.org/10.1038/nature02200

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