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- PDB-6kgx: Structure of the phycobilisome from the red alga Porphyridium pur... -
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Basic information
Entry | Database: PDB / ID: 6kgx | ||||||
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Title | Structure of the phycobilisome from the red alga Porphyridium purpureum | ||||||
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![]() | PHOTOSYNTHESIS / phycobilisome / Complex | ||||||
Function / homology | ![]() phycobilisome / chloroplast thylakoid membrane / photosynthesis / lyase activity Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.8 Å | ||||||
![]() | Sui, S.F. / Ma, J.F. / You, X. / Sun, S. | ||||||
![]() | ![]() Title: Structural basis of energy transfer in Porphyridium purpureum phycobilisome. Authors: Jianfei Ma / Xin You / Shan Sun / Xiaoxiao Wang / Song Qin / Sen-Fang Sui / ![]() Abstract: Photosynthetic organisms have developed various light-harvesting systems to adapt to their environments. Phycobilisomes are large light-harvesting protein complexes found in cyanobacteria and red ...Photosynthetic organisms have developed various light-harvesting systems to adapt to their environments. Phycobilisomes are large light-harvesting protein complexes found in cyanobacteria and red algae, 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 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. | ||||||
History |
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Structure visualization
Movie |
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Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 21.1 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 141.5 MB | Display | ![]() |
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Full document | ![]() | 142.4 MB | Display | |
Data in XML | ![]() | 3.8 MB | Display | |
Data in CIF | ![]() | 4.8 MB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9976MC ![]() 9977C ![]() 9978C ![]() 9979C ![]() 9980C ![]() 9981C ![]() 9982C ![]() 9983C ![]() 9984C ![]() 9985C ![]() 9986C ![]() 9987C ![]() 9988C 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 , 17 types, 580 molecules A1C1E1G1I1K1N1P1R1T1V1X1c1e1g1i1k1m1p1r1t1v1x1z1O2Q2S2U2W2Z2...
#1: Protein | Mass: 17824.029 Da / Num. of mol.: 254 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Protein | Mass: 18584.182 Da / Num. of mol.: 274 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Protein | Mass: 36924.992 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | Mass: 43968.605 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | Mass: 31332.955 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | Mass: 39727.625 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() #7: Protein | Mass: 31792.982 Da / Num. of mol.: 10 / Source method: isolated from a natural source / Source: (natural) ![]() #11: Protein | Mass: 32886.242 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein | Mass: 53601.336 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #13: Protein | Mass: 29453.639 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() #14: Protein | Mass: 31358.787 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #15: Protein | Mass: 37175.957 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #16: Protein | Mass: 55146.727 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #21: Protein | Mass: 10428.983 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #23: Protein | Mass: 16915.260 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #24: Protein | Mass: 30272.959 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #25: Protein | Mass: 26620.727 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Phycobilisome ... , 2 types, 8 molecules B2B6B7BBBFBIYH1H
#8: Protein | Mass: 26996.689 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() #22: Protein | Mass: 99468.367 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-C-phycocyanin ... , 2 types, 72 molecules C2E2G2I2K2M2C6E6G6I6K6M6C7E7G7I7K7M7CBEBGBIBKBMBCFEFGFIFKFMF...
#9: Protein | Mass: 17478.664 Da / Num. of mol.: 36 / Source method: isolated from a natural source / Source: (natural) ![]() #10: Protein | Mass: 18242.705 Da / Num. of mol.: 36 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Allophycocyanin ... , 4 types, 46 molecules AHCHEHGHJHKHNHPHRHTHcHeHgHiHlHmHpHrHtHvHDHFHBHHHIHLHMHOHQHSH...
#17: Protein | Mass: 17639.123 Da / Num. of mol.: 20 / Source method: isolated from a natural source / Source: (natural) ![]() #18: Protein | Mass: 17415.797 Da / Num. of mol.: 22 / Source method: isolated from a natural source / Source: (natural) ![]() #19: Protein | Mass: 18126.934 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #20: Protein | Mass: 19778.740 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 3 types, 1598 molecules ![](data/chem/img/PEB.gif)
![](data/chem/img/PUB.gif)
![](data/chem/img/CYC.gif)
![](data/chem/img/PUB.gif)
![](data/chem/img/CYC.gif)
#26: Chemical | ChemComp-PEB / #27: Chemical | ChemComp-PUB / #28: Chemical | ChemComp-CYC / |
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-Details
Has ligand of interest | N |
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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: Complex of phycobilisome from red alga P.purpureum. / Type: COMPLEX / Entity ID: #1-#25 / Source: NATURAL | ||||||||||||
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Source (natural) | Organism: ![]() | ||||||||||||
Buffer solution | pH: 7 | ||||||||||||
Buffer component |
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Specimen | Conc.: 1.5 mg/ml / Embedding applied: YES / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||
EM embedding | Material: ice | ||||||||||||
Vitrification | Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 298 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 / Nominal magnification: 105000 X / Nominal defocus max: 2200 nm / Nominal defocus min: 1200 nm / Cs: 0.001 mm / C2 aperture diameter: 70 µm |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Average exposure time: 5.6 sec. / Electron dose: 48 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of real images: 16218 |
EM imaging optics | Energyfilter name: GIF Quantum LS / Energyfilter slit width: 20 eV |
Image scans | Movie frames/image: 32 / Used frames/image: 1-32 |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING ONLY | ||||||||||||||||||
Particle selection | Num. of particles selected: 686369 | ||||||||||||||||||
Symmetry | Point symmetry: C2 (2 fold cyclic) | ||||||||||||||||||
3D reconstruction | Resolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 191825 / Symmetry type: POINT |