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题名: Structural organization of an intact phycobilisome and its association with photosystem II
作者: Chang, Leifu1, 2; Liu, Xianwei3; Li, Yanbing3; Liu, Cui-Cui1, 2; Yang, Fan1, 2; Zhao, Jindong3, 4; Sui, Sen-Fang1, 2
通讯作者: Zhao, JD (reprint author), Peking Univ, Coll Life Sci, State Key Lab Prot & Plant Genet Engn, Beijing 100871, Peoples R China.
关键词: phycobilisome ; photosynthesis ; phycobiliprotein ; electron microscopy
刊名: CELL RESEARCH
发表日期: 2015-06-01
DOI: 10.1038/cr.2015.59
卷: 25, 期:6, 页:726-737
收录类别: SCI
文章类型: Article
部门归属: [Chang, Leifu ; Liu, Cui-Cui ; Yang, Fan ; Sui, Sen-Fang] Tsinghua Univ, State Key Lab Biomembrane & Membrane Biotechnol, Beijing 100084, Peoples R China ; [Chang, Leifu ; Liu, Cui-Cui ; Yang, Fan ; Sui, Sen-Fang] Tsinghua Univ, Sch Life Sci, Ctr Struct Biol, Beijing 100084, Peoples R China ; [Liu, Xianwei ; Li, Yanbing ; Zhao, Jindong] Peking Univ, Coll Life Sci, State Key Lab Prot & Plant Genet Engn, Beijing 100871, Peoples R China ; [Zhao, Jindong] Chinese Acad Sci, Inst Hydrobiol, Key Lab Phycol, Wuhan 430072, Hubei, Peoples R China
WOS标题词: Science & Technology ; Life Sciences & Biomedicine
类目[WOS]: Cell Biology
研究领域[WOS]: Cell Biology
英文摘要: Phycobilisomes (PBSs) are light-harvesting antennae that transfer energy to photosynthetic reaction centers in cyanobacteria and red algae. PBSs are supermolecular complexes composed of phycobiliproteins (PBPs) that bear chromophores for energy absorption and linker proteins. Although the structures of some individual components have been determined using crystallography, the three-dimensional structure of an entire PBS complex, which is critical for understanding the energy transfer mechanism, remains unknown. Here, we report the structures of an intact PBS and a PBS in complex with photosystem II (PSII) from Anabaena sp. strain PCC 7120 using single-particle electron microscopy in combination with biochemical and molecular analyses. In the PBS structure, all PBP trimers and the conserved linker protein domains were unambiguously located, and the global distribution of all chromophores was determined. We provide evidence that ApcE and ApcF are critical for the formation of a protrusion at the bottom of PBS, which plays an important role in mediating PBS interaction with PSII. Our results provide insights into the molecular architecture of an intact PBS at different assembly levels and provide the basis for understanding how the light energy absorbed by PBS is transferred to PSII.
关键词[WOS]: ALLOPHYCOCYANIN CORE COMPLEX ; CRYSTAL-STRUCTURE ; CYANOBACTERIAL PHYCOBILISOMES ; ELECTRON-MICROSCOPY ; C-PHYCOCYANIN ; MASTIGOCLADUS-LAMINOSUS ; PORPHYRIDIUM-CRUENTUM ; ENERGY-TRANSFER ; PCC 7120 ; RESOLUTION
语种: 英语
WOS记录号: WOS:000355554800009
ISSN号: 1001-0602
Citation statistics:
内容类型: 期刊论文
URI标识: http://ir.ihb.ac.cn/handle/342005/23971
Appears in Collections:水生生物分子与细胞生物学研究中心_期刊论文

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作者单位: 1.Tsinghua Univ, State Key Lab Biomembrane & Membrane Biotechnol, Beijing 100084, Peoples R China
2.Tsinghua Univ, Sch Life Sci, Ctr Struct Biol, Beijing 100084, Peoples R China
3.Peking Univ, Coll Life Sci, State Key Lab Prot & Plant Genet Engn, Beijing 100871, Peoples R China
4.Chinese Acad Sci, Inst Hydrobiol, Key Lab Phycol, Wuhan 430072, Hubei, Peoples R China
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