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Crystal structure of plant photosystem I

Author

Listed:
  • Adam Ben-Shem

    (The George S. Wise Faculty of Life Sciences, Tel Aviv University)

  • Felix Frolow

    (The George S. Wise Faculty of Life Sciences, Tel Aviv University)

  • Nathan Nelson

    (The George S. Wise Faculty of Life Sciences, Tel Aviv University)

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.

Suggested Citation

  • Adam Ben-Shem & Felix Frolow & Nathan Nelson, 2003. "Crystal structure of plant photosystem I," Nature, Nature, vol. 426(6967), pages 630-635, December.
    • Handle: RePEc:nat:nature:v:426:y:2003:i:6967:d:10.1038_nature02200
    DOI: 10.1038/nature02200
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    Cited by:

    1. Makiko Kosugi & Masato Kawasaki & Yutaka Shibata & Kojiro Hara & Shinichi Takaichi & Toshio Moriya & Naruhiko Adachi & Yasuhiro Kamei & Yasuhiro Kashino & Sakae Kudoh & Hiroyuki Koike & Toshiya Senda, 2023. "Uphill energy transfer mechanism for photosynthesis in an Antarctic alga," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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