Ma, Jianfei; You, Xin; Sun, Shan; Wang, Xiaoxiao; Qin, Song
; Sui, Sen-Fang发表期刊NATURE
2020
关键词CRYO-EMCYANOBACTERIAL PHYCOBILISOMESALLOPHYCOCYANIN BCRYSTAL-STRUCTURER-PHYCOCYANINPHYCOERYTHRINCRUENTUMPIGMENTCHROMOPHORESORGANIZATION
研究领域Multidisciplinary Sciences
DOI10.1038/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
作者部门海岸带生物学与生物资源保护实验室
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.
文章类型Article; Early Access
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]
收录类别SCI
语种英语
关键词[WOS]CRYO-EM; CYANOBACTERIAL PHYCOBILISOMES; ALLOPHYCOCYANIN B; CRYSTAL-STRUCTURE; R-PHYCOCYANIN; PHYCOERYTHRIN; CRUENTUM; PIGMENT; CHROMOPHORES; ORGANIZATION
WOS记录号WOS:000517050000005
引用统计被引频次：34[WOS][WOS记录][WOS相关记录]
文献类型期刊论文
条目标识符http://ir.yic.ac.cnhttp://ir.yic.ac.cn/handle/133337/25085
专题海岸带生物学与生物资源利用重点实验室_海岸带生物学与生物资源保护实验室
作者单位1.Tsinghua Univ, Sch Life Sci, Beijing Adv Innovat Ctr Struct Biol, State Key Lab Membrane Biol, Beijing, Peoples R China;
2.Chinese Acad Sci, Yantai Inst Coast Zone Res, Yantai, Peoples R China
推荐引用方式
GB/T 7714Ma, Jianfei,You, Xin,Sun, Shan,et al. Structural basis of energy transfer in Porphyridium purpureum phycobilisome[J]. NATURE,2020.
APAMa, Jianfei,You, Xin,Sun, Shan,Wang, Xiaoxiao,Qin, Song,&Sui, Sen-Fang.(2020).Structural basis of energy transfer in Porphyridium purpureum phycobilisome.NATURE.
MLAMa, Jianfei,et al."Structural basis of energy transfer in Porphyridium purpureum phycobilisome".NATURE (2020).
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