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Structural insights into energy regulation of light-harvesting complex CP29 from spinach

Nature Structural & Molecular Biology volume 18, pages 309–315 (2011)Cite this article

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Abstract

CP29, one of the minor light-harvesting complexes of higher-plant photosystem II, absorbs and transfers solar energy for photosynthesis and also has important roles in photoprotection. We have solved the crystal structure of spinach CP29 at 2.80-Å resolution. Each CP29 monomer contains 13 chlorophyll and 3 carotenoid molecules, which differs considerably from the major light-harvesting complex LHCII and the previously proposed CP29 model. The 13 chlorophyll-binding sites are assigned as eight chlorophyll a sites, four chlorophyll b and one putative mixed site occupied by both chlorophylls a and b. Based on the present X-ray structure, an integrated pigment network in CP29 is constructed. Two special clusters of pigment molecules, namely a615–a611–a612–Lut and Vio(Zea)–a603–a609, have been identified and might function as potential energy-quenching centers and as the exit or entrance in energy-transfer pathways.

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Figure 1: Stereo view of the overall structure of CP29.
Figure 2: Structural comparison between CP29 and LHCII (PDB 1RWT)4.
Figure 3: Room temperature (20 °C) absorption spectra of CP29 showing its characteristic features.
Figure 4: Pigment arrangement in CP29.
Figure 5: Strongly interacting pigment cluster a615–a611–a612–Lut.
Figure 6: Pigment cluster Vio(Zea)–a603–a609.
Figure 7: Two important pigment clusters in CP29.

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Acknowledgements

We thank D.C. Liang, X.C. Gu, R. Bassi, N. Isaacs and T. Jiang for discussions and the staffs at the Shanghai Synchrotron Radiation Facility, the Beijing Synchrotron Radiation Facility, SPring8 and the Photo Factory for technical support with crystal screening and data collection. This work was supported by National Natural Science Foundation of China grants 30530210, 30721003 and 31021062 (W.R.C.), 973 Project grants 2006CB806505, 2006CB911001 and 2011CBA00902 (W.R.C.) and Knowledge Innovation Program of the Chinese Academy of Sciences grant KSCX2-YW-R-123 (W.R.C.).

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Authors and Affiliations

  1. National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China

    Xiaowei Pan, Mei Li, Tao Wan, Longfei Wang, Chenjun Jia, Zhiqiang Hou, Xuelin Zhao, Jiping Zhang & Wenrui Chang

  2. Graduate University of the Chinese Academy of Sciences, Beijing, China

    Tao Wan, Longfei Wang, Chenjun Jia & Zhiqiang Hou

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Contributions

X.W.P. did the purification, crystallization, data collection and processing, structure determination and structural analysis. M.L. assisted in data collection, structure analysis and manuscript preparation. T.W. did the protein sequence determination. L.F.W. assisted in data collection and structure determination. C.J.J., Z.Q.H., X.L.Z. and J.P.Z. assisted in sample isolation and purification. W.R.C. supervised the project and analyzed the structure. X.W.P. and W.R.C. wrote the manuscript.

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Correspondence to Wenrui Chang.

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Pan, X., Li, M., Wan, T. et al. Structural insights into energy regulation of light-harvesting complex CP29 from spinach. Nat Struct Mol Biol 18, 309–315 (2011). https://doi.org/10.1038/nsmb.2008

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