Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution

Zhenfeng Liu, Hanchi Yan, Kebin Wang, Tingyun Kuang, Jiping Zhang, Lulu Gui, Xiaomin An and Wenrui Chang ()
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Zhenfeng Liu: Institute of Biophysics, Chinese Academy of Sciences
Hanchi Yan: Institute of Biophysics, Chinese Academy of Sciences
Kebin Wang: Institute of Botany, Chinese Academy of Sciences
Tingyun Kuang: Institute of Botany, Chinese Academy of Sciences
Jiping Zhang: Institute of Biophysics, Chinese Academy of Sciences
Lulu Gui: Institute of Biophysics, Chinese Academy of Sciences
Xiaomin An: Institute of Biophysics, Chinese Academy of Sciences
Wenrui Chang: Institute of Biophysics, Chinese Academy of Sciences

Nature, 2004, vol. 428, issue 6980, 287-292

Abstract: Abstract The major light-harvesting complex of photosystem II (LHC-II) serves as the principal solar energy collector in the photosynthesis of green plants and presumably also functions in photoprotection under high-light conditions. Here we report the first X-ray structure of LHC-II in icosahedral proteoliposome assembly at atomic detail. One asymmetric unit of a large R32 unit cell contains ten LHC-II monomers. The 14 chlorophylls (Chl) in each monomer can be unambiguously distinguished as eight Chla and six Chlb molecules. Assignment of the orientation of the transition dipole moment of each chlorophyll has been achieved. All Chlb are located around the interface between adjacent monomers, and together with Chla they are the basis for efficient light harvesting. Four carotenoid-binding sites per monomer have been observed. The xanthophyll-cycle carotenoid at the monomer–monomer interface may be involved in the non-radiative dissipation of excessive energy, one of the photoprotective strategies that have evolved in plants.

Date: 2004
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DOI: 10.1038/nature02373

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