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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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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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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DOI: https://doi.org/10.1038/nature02200
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