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- PDB-5y6p: Structure of the phycobilisome from the red alga Griffithsia pacifica -
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Open data
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Basic information
Entry | Database: PDB / ID: 5y6p | ||||||
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Title | Structure of the phycobilisome from the red alga Griffithsia pacifica | ||||||
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![]() | PHOTOSYNTHESIS / phycobilisome | ||||||
Function / homology | PHYCOCYANOBILIN / PHYCOERYTHROBILIN / PHYCOUROBILIN / PHYCOVIOLOBILIN![]() | ||||||
Biological species | ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å | ||||||
![]() | Zhang, J. / Ma, J.F. / Liu, D.S. / Sun, S. / Sui, S.F. | ||||||
![]() | ![]() Title: Structure of phycobilisome from the red alga Griffithsia pacifica. Authors: Jun Zhang / Jianfei Ma / Desheng Liu / Song Qin / Shan Sun / Jindong Zhao / Sen-Fang Sui / ![]() 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 ...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. | ||||||
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 28.7 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 190.7 MB | Display | ![]() |
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Full document | ![]() | 188.5 MB | Display | |
Data in XML | ![]() | 4.4 MB | Display | |
Data in CIF | ![]() | 5.6 MB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6769MC ![]() 6758C ![]() 6759C ![]() 6760C ![]() 6761C ![]() 6762C ![]() 6763C ![]() 6764C ![]() 6765C ![]() 6766C ![]() 6767C ![]() 6768C M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
+Protein , 23 types, 190 molecules A1B1C1D1E1F1G1I1K1N1P1R1T1X1Z1b1d1f1i1k1o1q1s1u1w1y1H1J1L1M1...
-R-phycoerythrin ... , 2 types, 672 molecules e2g2i2k2m2o2q2s2u2w2y2E2G2I2K2M2O2Q2S2U2W2Y2A3C3E3G3I3K3M3O3...
#10: Protein | Mass: 17763.820 Da / Num. of mol.: 326 / Source method: isolated from a natural source / Source: (natural) ![]() #11: Protein | Mass: 18496.031 Da / Num. of mol.: 346 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 4 types, 2048 molecules ![](data/chem/img/PEB.gif)
![](data/chem/img/CYC.gif)
![](data/chem/img/PUB.gif)
![](data/chem/img/PVN.gif)
![](data/chem/img/CYC.gif)
![](data/chem/img/PUB.gif)
![](data/chem/img/PVN.gif)
#26: Chemical | ChemComp-PEB / #27: Chemical | ChemComp-CYC / #28: Chemical | ChemComp-PUB / #29: Chemical | ChemComp-PVN / |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: phycobilisome / Type: COMPLEX / Entity ID: #1-#25 / Source: NATURAL |
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Molecular weight | Value: 16.8 MDa / Experimental value: NO |
Source (natural) | Organism: ![]() |
Buffer solution | pH: 7 |
Specimen | Conc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 289.15 K |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
CTF correction | Type: NONE |
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3D reconstruction | Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 53403 / Symmetry type: POINT |