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Yorodumi- PDB-7dz7: State transition supercomplex PSI-LHCI-LHCII from double phosphat... -
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-Basic information
Entry | Database: PDB / ID: 7dz7 | |||||||||||||||||||||||||||
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Title | State transition supercomplex PSI-LHCI-LHCII from double phosphatase mutant pph1;pbcp of green alga Chlamydomonas reinhardtii | |||||||||||||||||||||||||||
Components |
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Keywords | PHOTOSYNTHESIS / Supercomplex / state transition / green alga / Chlamydomonas reinhardtii | |||||||||||||||||||||||||||
Function / homology | Function and homology information chloroplast thylakoid lumen / photosynthesis, light harvesting / photosynthesis, light harvesting in photosystem I / photosystem I reaction center / photosystem I / photosynthetic electron transport in photosystem I / photosystem I / photosystem II / chlorophyll binding / chloroplast thylakoid membrane ...chloroplast thylakoid lumen / photosynthesis, light harvesting / photosynthesis, light harvesting in photosystem I / 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 | Chlamydomonas reinhardtii (plant) | |||||||||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.84 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: 2021 Title: 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. | |||||||||||||||||||||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 7dz7.cif.gz | 1.5 MB | Display | PDBx/mmCIF format |
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PDB format | pdb7dz7.ent.gz | 1.3 MB | Display | PDB format |
PDBx/mmJSON format | 7dz7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7dz7_validation.pdf.gz | 23.8 MB | Display | wwPDB validaton report |
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Full document | 7dz7_full_validation.pdf.gz | 24.8 MB | Display | |
Data in XML | 7dz7_validation.xml.gz | 323 KB | Display | |
Data in CIF | 7dz7_validation.cif.gz | 386.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dz/7dz7 ftp://data.pdbj.org/pub/pdb/validation_reports/dz/7dz7 | HTTPS FTP |
-Related structure data
Related structure data | 30925MC 7dz8C 7e0hC 7e0iC 7e0jC 7e0kC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-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) Chlamydomonas reinhardtii (plant) / References: UniProt: P12154, photosystem I |
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#2: Protein | Mass: 82184.266 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: P09144, photosystem I |
#3: Protein | Mass: 8869.325 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q00914, photosystem I |
#4: Protein | Mass: 21372.887 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q39615 |
#5: Protein | Mass: 10786.395 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: P12352 |
#6: Protein | Mass: 24088.936 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: P12356 |
#7: Protein | Mass: 13236.007 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: P14224 |
#8: Protein | Mass: 14173.131 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: P13352 |
#9: Protein | Mass: 10586.388 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8IFG7 |
#10: Protein/peptide | Mass: 4750.509 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: P59777 |
#11: Protein | Mass: 11214.084 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: P14225 |
#13: Protein | Mass: 13753.862 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8JCL6 |
-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) Chlamydomonas reinhardtii (plant) / References: UniProt: A8IL32 |
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-Chlorophyll a-b binding protein, ... , 13 types, 16 molecules a123456789XWYUZV
#14: Protein | Mass: 23923.205 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q05093 #15: Protein | | Mass: 26951.219 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8IKC8 #16: Protein | | Mass: 32629.486 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8JF10 #17: Protein | | Mass: 28729.822 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q75VZ0 #18: Protein | | Mass: 28257.555 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q75VY8 #19: Protein | | Mass: 27812.373 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q75VY6 #20: Protein | | Mass: 26248.869 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q84Y02 #21: Protein | | Mass: 25948.812 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q75VY7 #22: Protein | | Mass: 22867.277 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8ITV3 #23: Protein | Mass: 26675.350 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q93WE0 #24: Protein | Mass: 27405.008 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q93WL4 #25: Protein | | Mass: 27671.316 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q93VE0 #26: Protein | | Mass: 28796.824 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q9ZSJ4 |
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-Sugars , 2 types, 8 molecules
#32: Sugar | ChemComp-LMU / #34: Sugar | ChemComp-DGD / | |
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-Non-polymers , 10 types, 463 molecules
#27: Chemical | ChemComp-CLA / #28: Chemical | #29: Chemical | ChemComp-LHG / #30: Chemical | ChemComp-BCR / #31: Chemical | #33: Chemical | ChemComp-LMG / #35: Chemical | ChemComp-LUT / ( #36: Chemical | ChemComp-XAT / ( #37: Chemical | ChemComp-NEX / ( #38: 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 |
-Sample preparation
Component | Name: State transition complex PSI-LHCI-LHCII from green algae Type: COMPLEX / Entity ID: #1-#26 / Source: NATURAL |
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Molecular weight | Experimental value: YES |
Source (natural) | Organism: Chlamydomonas reinhardtii (plant) |
Buffer solution | pH: 6.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-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) |
-Processing
Software | Name: PHENIX / Version: 1.17.1_3660: / Classification: refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 2.84 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 56601 / Symmetry type: POINT | ||||||||||||||||||||||||
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