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Yorodumi- PDB-7dz8: State transition supercomplex PSI-LHCI-LHCII from the LhcbM1 lack... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 7dz8 | ||||||||||||||||||||||||||||||||||||
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| Title | State transition supercomplex PSI-LHCI-LHCII from the LhcbM1 lacking mutant of Chlamydomonas reinhardtii | ||||||||||||||||||||||||||||||||||||
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Keywords | PHOTOSYNTHESIS / Supercomplex / state transition / green alga / Chlamydomonas reinhardtii | ||||||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationphotosynthesis, light harvesting in photosystem I / chloroplast thylakoid lumen / photosynthesis, light harvesting / photosystem I reaction center / photosystem I / photosynthetic electron transport in photosystem I / photosystem I / photosystem II / chlorophyll binding / chloroplast thylakoid membrane ...photosynthesis, light harvesting in photosystem I / chloroplast thylakoid lumen / photosynthesis, light harvesting / photosystem I reaction center / photosystem I / photosynthetic electron transport in photosystem I / photosystem I / photosystem II / chlorophyll binding / chloroplast thylakoid membrane / response to light stimulus / photosynthesis / 4 iron, 4 sulfur cluster binding / electron transfer activity / oxidoreductase activity / magnesium ion binding / metal ion binding Similarity search - Function | ||||||||||||||||||||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.16 Å | ||||||||||||||||||||||||||||||||||||
Authors | Pan, X.W. / Li, A.J. / Liu, Z.F. / Li, M. | ||||||||||||||||||||||||||||||||||||
| Funding support | China, Japan, 8items
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Citation | Journal: Nat Plants / Year: 2021Title: Structural basis of LhcbM5-mediated state transitions in green algae. Authors: Xiaowei Pan / Ryutaro Tokutsu / Anjie Li / Kenji Takizawa / Chihong Song / Kazuyoshi Murata / Tomohito Yamasaki / Zhenfeng Liu / Jun Minagawa / Mei Li / ![]() Abstract: In green algae and plants, state transitions serve as a short-term light-acclimation process in the regulation of the light-harvesting capacity of photosystems I and II (PSI and PSII, respectively). ...In green algae and plants, state transitions serve as a short-term light-acclimation process in the regulation of the light-harvesting capacity of photosystems I and II (PSI and PSII, respectively). During the process, a portion of light-harvesting complex II (LHCII) is phosphorylated, dissociated from PSII and binds with PSI to form the supercomplex PSI-LHCI-LHCII. Here, we report high-resolution structures of PSI-LHCI-LHCII from Chlamydomonas reinhardtii, revealing the mechanism of assembly between the PSI-LHCI complex and two phosphorylated LHCII trimers containing all four types of LhcbM protein. Two specific LhcbM isoforms, namely LhcbM1 and LhcbM5, directly interact with the PSI core through their phosphorylated amino terminal regions. Furthermore, biochemical and functional studies on mutant strains lacking either LhcbM1 or LhcbM5 indicate that only LhcbM5 is indispensable in supercomplex formation. The results unravel the specific interactions and potential excitation energy transfer routes between green algal PSI and two phosphorylated LHCIIs. | ||||||||||||||||||||||||||||||||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 7dz8.cif.gz | 1.5 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb7dz8.ent.gz | 1.3 MB | Display | PDB format |
| PDBx/mmJSON format | 7dz8.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dz/7dz8 ftp://data.pdbj.org/pub/pdb/validation_reports/dz/7dz8 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 30926MC ![]() 7dz7C ![]() 7e0hC ![]() 7e0iC ![]() 7e0jC ![]() 7e0kC 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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| 1 |
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Components
-Photosystem I ... , 12 types, 12 molecules ABCDEFGHIJKO
| #1: Protein | Mass: 83239.203 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #2: Protein | Mass: 82184.266 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #3: Protein | Mass: 8869.325 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #4: Protein | Mass: 21372.887 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #5: Protein | Mass: 10786.395 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #6: Protein | Mass: 24088.936 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #7: Protein | Mass: 13236.007 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #8: Protein | Mass: 14173.131 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #9: Protein | Mass: 10586.388 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein/peptide | Mass: 4750.509 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #11: Protein | Mass: 11214.084 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #13: Protein | Mass: 13753.862 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein , 1 types, 1 molecules L
| #12: Protein | Mass: 20300.539 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Chlorophyll a-b binding protein, ... , 12 types, 16 molecules 1a23456789XWYZUV
| #14: Protein | Mass: 23923.205 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #15: Protein | | Mass: 26951.219 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #16: Protein | | Mass: 32629.486 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #17: Protein | | Mass: 28729.822 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #18: Protein | | Mass: 28257.555 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #19: Protein | | Mass: 27812.373 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #20: Protein | | Mass: 26248.869 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #21: Protein | | Mass: 25948.812 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #22: Protein | | Mass: 22867.277 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #23: Protein | Mass: 26675.350 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #24: Protein | Mass: 27405.008 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #25: Protein | | Mass: 28796.824 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Sugars , 2 types, 8 molecules 


| #31: Sugar | ChemComp-LMU / #33: Sugar | ChemComp-DGD / | |
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-Non-polymers , 10 types, 463 molecules 


















| #26: Chemical | ChemComp-CLA / #27: Chemical | #28: Chemical | ChemComp-LHG / #29: Chemical | ChemComp-BCR / #30: Chemical | #32: Chemical | ChemComp-LMG / #34: Chemical | ChemComp-LUT / ( #35: Chemical | ChemComp-XAT / ( #36: Chemical | ChemComp-NEX / ( #37: Chemical | ChemComp-CHL / |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | Y |
-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: State transition complex PSI-LHCI-LHCII from green algae Type: COMPLEX / Entity ID: #1-#25 / Source: NATURAL |
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| Molecular weight | Experimental value: YES |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 6.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TALOS ARCTICA |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD |
| Image recording | Electron dose: 1.5625 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
| Software | Name: PHENIX / Version: 1.17.1_3660: / Classification: refinement | ||||||||||||||||||||||||
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| EM software | Name: PHENIX / Category: model refinement | ||||||||||||||||||||||||
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.16 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 123997 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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