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Yorodumi- PDB-9iox: Cryo-EM structure of a TEF30-associated intermediate PSII core di... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9iox | ||||||||||||||||||||||||
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| Title | Cryo-EM structure of a TEF30-associated intermediate PSII core dimer complex, type II, from Chlamydomonas reinhardtii | ||||||||||||||||||||||||
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Keywords | PHOTOSYNTHESIS / photosystem II / PSII repair / PSII assembly / PSII intermediate / TEF30 | ||||||||||||||||||||||||
| Function / homology | Function and homology informationoxygen evolving activity / photosystem II stabilization / photosystem II reaction center / photosystem II / oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor / photosynthetic electron transport chain / photosystem II / response to herbicide / chlorophyll binding / photosynthetic electron transport in photosystem II ...oxygen evolving activity / photosystem II stabilization / photosystem II reaction center / photosystem II / oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor / photosynthetic electron transport chain / photosystem II / response to herbicide / chlorophyll binding / photosynthetic electron transport in photosystem II / : / phosphate ion binding / chloroplast thylakoid membrane / photosynthesis, light reaction / photosynthesis / electron transfer activity / protein stabilization / iron ion binding / heme binding / metal ion binding Similarity search - Function | ||||||||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | ||||||||||||||||||||||||
Authors | Wang, Y. / Wang, C. / Li, A. / Liu, Z. | ||||||||||||||||||||||||
| Funding support | China, 1items
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Citation | Journal: Nat Plants / Year: 2025Title: Roles of multiple TEF30-associated intermediate complexes in the repair and reassembly of photosystem II in Chlamydomonas reinhardtii. Authors: Yidi Wang / Chenxi Wang / Anjie Li / Zhenfeng Liu / ![]() Abstract: During oxygenic photosynthesis, photosystem II (PSII) uses light energy for oxidizing water and reducing plastoquinone. It is susceptible to photodamage, and the damaged PSII is repaired through a ...During oxygenic photosynthesis, photosystem II (PSII) uses light energy for oxidizing water and reducing plastoquinone. It is susceptible to photodamage, and the damaged PSII is repaired through a sophisticated biological process assisted by numerous auxiliary proteins. Here we report the cryogenic electron microscopy structures of four PSII-repair complexes from Chlamydomonas reinhardtii associated with the Thylakoid Enriched Fraction 30 (TEF30, an orthologue of plant MET1) protein-namely, a TEF30-PSII core monomer (TEF30-C), two types of TEF30-PSII core dimers (types I and II, TEF30-C-I and TEF30-C-II) and a TEF30-CS-type PSII-LHCII supercomplex (TEF30-CS; S, strongly associated light-harvesting complex II trimer). TEF30 mediates the assembly of CP43 with the RC47 module by clamping on the stromal surfaces and prevents the premature association of peripheral antennae with PSII-C. In the transition from TEF30-C-I to TEF30-C-II, TEF30-CS and mature CS, one PSII core slides along the dimerization interface against the adjacent one by 22-35 Å, generating a zigzagged surface for accommodating the peripheral antennae. These results suggest that the PSII repair process undergoes multiple TEF30-mediated intermediate states to form intact PSII-LHCII supercomplexes. | ||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9iox.cif.gz | 922.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9iox.ent.gz | 789.3 KB | Display | PDB format |
| PDBx/mmJSON format | 9iox.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9iox_validation.pdf.gz | 6.5 MB | Display | wwPDB validaton report |
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| Full document | 9iox_full_validation.pdf.gz | 6.8 MB | Display | |
| Data in XML | 9iox_validation.xml.gz | 176.2 KB | Display | |
| Data in CIF | 9iox_validation.cif.gz | 235.2 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/io/9iox ftp://data.pdbj.org/pub/pdb/validation_reports/io/9iox | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 60748MC ![]() 9iiuC ![]() 9imnC ![]() 9is4C M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-Photosystem II ... , 12 types, 24 molecules AaBbCcDdHhIiKkLlMmTtVvZz
| #1: Protein | Mass: 36263.301 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Protein | Mass: 52938.281 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Protein | Mass: 49473.355 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | Mass: 39342.836 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #8: Protein | Mass: 7751.167 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein/peptide | Mass: 3902.687 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #10: Protein/peptide | Mass: 4147.979 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #11: Protein/peptide | Mass: 4431.229 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein/peptide | Mass: 2971.595 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #13: Protein/peptide | Mass: 3265.905 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #14: Protein/peptide | Mass: 3087.760 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #16: Protein | Mass: 6466.732 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Cytochrome b559 subunit ... , 2 types, 4 molecules EeFf
| #5: Protein | Mass: 8484.632 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein/peptide | Mass: 3535.273 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Protein / Protein/peptide , 2 types, 4 molecules GgXx
| #15: Protein/peptide | Mass: 3056.640 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #7: Protein | Mass: 22399.248 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Sugars , 2 types, 8 molecules 


| #24: Sugar | ChemComp-DGD / #25: Sugar | |
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-Non-polymers , 10 types, 128 molecules 


















| #17: Chemical | | #18: Chemical | ChemComp-CLA / #19: Chemical | ChemComp-PHO / #20: Chemical | ChemComp-BCR / #21: Chemical | ChemComp-LMG / #22: Chemical | ChemComp-LHG / #23: Chemical | #26: Chemical | #27: Chemical | #28: Chemical | |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | N |
-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: TEF30-associated PSII core dimer complex, type II / Type: COMPLEX / Entity ID: #1-#16 / Source: NATURAL |
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| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.2 |
| 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: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1800 nm / Nominal defocus min: 1300 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING ONLY |
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| 3D reconstruction | Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 33509 / Symmetry type: POINT |
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FIELD EMISSION GUN