Structure of phycobilisome from the red alga Griffithsia pacifica

Jun Zhang, Jianfei Ma, Desheng Liu, Song Qin, Shan Sun (), Jindong Zhao and Sen-Fang Sui ()
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Jun Zhang: State Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University
Jianfei Ma: State Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University
Desheng Liu: State Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University
Song Qin: Yantai Institute of Coast Zone Research, Chinese Academy of Sciences
Shan Sun: State Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University
Jindong Zhao: State Key Laboratory of Protein and Plant Genetic Engineering, College of Life Sciences, Peking University
Sen-Fang Sui: State Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University

Nature, 2017, vol. 551, issue 7678, 57-63

Abstract: Abstract Life on Earth depends on photosynthesis for its conversion of solar energy to chemical energy. Photosynthetic organisms have developed a variety of light-harvesting systems to capture sunlight. The largest light-harvesting complex is the phycobilisome (PBS), the main light-harvesting antenna in cyanobacteria and red algae. It is composed of phycobiliproteins and linker proteins but the assembly mechanisms and energy transfer pathways of the PBS are not well understood. Here we report the structure of a 16.8-megadalton PBS from a red alga at 3.5 Å resolution obtained by single-particle cryo-electron microscopy. We modelled 862 protein subunits, including 4 linkers in the core, 16 rod–core linkers and 52 rod linkers, and located a total of 2,048 chromophores. This structure reveals the mechanisms underlying specific interactions between linkers and phycobiliproteins, and the formation of linker skeletons. These results provide a firm structural basis for our understanding of complex assembly and the mechanisms of energy transfer within the PBS.

Date: 2017
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DOI: 10.1038/nature24278

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