Structural basis of energy transfer in Porphyridium purpureum phycobilisome
文献类型：期刊论文
| 作者 | Ma, Jianfei; You, Xin; Sun, Shan; Wang, Xiaoxiao; Qin, Song ; Sui, Sen-Fang
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| 刊名 | NATURE
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| 出版日期 | 2020 |
| 关键词 | CRYO-EM CYANOBACTERIAL PHYCOBILISOMES ALLOPHYCOCYANIN B CRYSTAL-STRUCTURE R-PHYCOCYANIN PHYCOERYTHRIN CRUENTUM PIGMENT CHROMOPHORES ORGANIZATION |
| DOI | 10.1038/s41586-020-2020-7 |
| 产权排序 | [Ma, Jianfei ; You, Xin ; Sun, Shan ; Sui, Sen-Fang] Tsinghua Univ, Sch Life Sci, Beijing Adv Innovat Ctr Struct Biol, State Key Lab Membrane Biol, Beijing, Peoples R China ; [Wang, Xiaoxiao ; Qin, Song] Chinese Acad Sci, Yantai Inst Coast Zone Res, Yantai, Peoples R China |
| 文献子类 | Article; Early Access |
| 英文摘要 | The cryo-electron microscopy structure of a phycobilisome from the red alga Porphyridium purpureum reveals how aromatic interactions between the linker proteins and the chromophores drive a unidirectional transfer of energy. Photosynthetic organisms have developed various light-harvesting systems to adapt to their environments(1). Phycobilisomes are large light-harvesting protein complexes found in cyanobacteria and red algae(2-4), although how the energies of the chromophores within these complexes are modulated by their environment is unclear. Here we report the cryo-electron microscopy structure of a 14.7-megadalton phycobilisome with a hemiellipsoidal shape from the red alga Porphyridium purpureum. Within this complex we determine the structures of 706 protein subunits, including 528 phycoerythrin, 72 phycocyanin, 46 allophycocyanin and 60 linker proteins. In addition, 1,598 chromophores are resolved comprising 1,430 phycoerythrobilin, 48 phycourobilin and 120 phycocyanobilin molecules. The markedly improved resolution of our structure compared with that of the phycobilisome of Griffithsia pacifica(5) enabled us to build an accurate atomic model of the P. purpureum phycobilisome system. The model reveals how the linker proteins affect the microenvironment of the chromophores, and suggests that interactions of the aromatic amino acids of the linker proteins with the chromophores may be a key factor in fine-tuning the energy states of the chromophores to ensure the efficient unidirectional transfer of energy. |
| WOS关键词 | CRYO-EM ; CYANOBACTERIAL PHYCOBILISOMES ; ALLOPHYCOCYANIN B ; CRYSTAL-STRUCTURE ; R-PHYCOCYANIN ; PHYCOERYTHRIN ; CRUENTUM ; PIGMENT ; CHROMOPHORES ; ORGANIZATION |
| 语种 | 英语 |
| WOS记录号 | WOS:000517050000005 |
| 资助机构 | National Basic Research ProgramNational Basic Research Program of China [2016YFA0501101, 2017YFA0504600] ; National Natural Science Foundation of ChinaNational Natural Science Foundation of China [31670745, 31861143048] |
| 源URL | [http://ir.yic.ac.cn/handle/133337/25085]  |
| 专题 | 烟台海岸带研究所_海岸带生物学与生物资源利用所重点实验室 |
| 作者单位 | 1.Chinese Acad Sci, Yantai Inst Coast Zone Res, Yantai, Peoples R China 2.Tsinghua Univ, Sch Life Sci, Beijing Adv Innovat Ctr Struct Biol, State Key Lab Membrane Biol, Beijing, Peoples R China; |
| 推荐引用方式 GB/T 7714 | Ma, Jianfei,You, Xin,Sun, Shan,et al. Structural basis of energy transfer in Porphyridium purpureum phycobilisome[J]. NATURE,2020. |
| APA | Ma, Jianfei,You, Xin,Sun, Shan,Wang, Xiaoxiao,Qin, Song,&Sui, Sen-Fang.(2020).Structural basis of energy transfer in Porphyridium purpureum phycobilisome.NATURE. |
| MLA | Ma, Jianfei,et al."Structural basis of energy transfer in Porphyridium purpureum phycobilisome".NATURE (2020). |
入库方式： OAI收割
来源：烟台海岸带研究所
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