[English] 日本語
Yorodumi- PDB-9iiu: Cryo-EM structure of an TEF30-associated intermediate PSII core c... -
+
Open data
-
Basic information
| Entry | Database: PDB / ID: 9iiu | ||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Title | Cryo-EM structure of an TEF30-associated intermediate PSII core complex from Chlamydomonas reinhardtii | ||||||||||||||||||||||||
Components |
| ||||||||||||||||||||||||
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 ...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 / photosynthesis, light reaction / chloroplast thylakoid membrane / 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: 2.98 Å | ||||||||||||||||||||||||
Authors | Wang, Y. / Wang, C. / Li, A. / Liu, Z. | ||||||||||||||||||||||||
| Funding support | China, 1items
| ||||||||||||||||||||||||
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. | ||||||||||||||||||||||||
| History |
|
-
Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
|---|
-
Downloads & links
-
Download
| PDBx/mmCIF format | 9iiu.cif.gz | 551.8 KB | Display | PDBx/mmCIF format |
|---|---|---|---|---|
| PDB format | pdb9iiu.ent.gz | 454 KB | Display | PDB format |
| PDBx/mmJSON format | 9iiu.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9iiu_validation.pdf.gz | 4 MB | Display | wwPDB validaton report |
|---|---|---|---|---|
| Full document | 9iiu_full_validation.pdf.gz | 4.2 MB | Display | |
| Data in XML | 9iiu_validation.xml.gz | 99.6 KB | Display | |
| Data in CIF | 9iiu_validation.cif.gz | 136.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ii/9iiu ftp://data.pdbj.org/pub/pdb/validation_reports/ii/9iiu | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 60605MC ![]() 9imnC ![]() 9ioxC ![]() 9is4C M: map data used to model this data C: citing same article ( |
|---|---|
| Similar structure data | Similarity search - Function & homology F&H Search |
-
Links
-
Assembly
| Deposited unit | ![]()
|
|---|---|
| 1 |
|
-
Components
-Photosystem II ... , 13 types, 13 molecules ABCDHIJKLMTVZ
| #1: Protein | Mass: 36192.223 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
|---|---|
| #2: Protein | Mass: 52938.281 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #3: Protein | Mass: 49473.355 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #4: Protein | Mass: 39128.578 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #8: Protein | Mass: 7652.035 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #9: Protein/peptide | Mass: 3902.687 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein/peptide | Mass: 3270.858 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #11: Protein/peptide | Mass: 4147.979 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #12: Protein/peptide | Mass: 4071.762 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #13: Protein/peptide | Mass: 2971.595 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #14: Protein/peptide | Mass: 2799.394 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #15: Protein/peptide | Mass: 3201.863 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #17: Protein | Mass: 6466.732 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Cytochrome b559 subunit ... , 2 types, 2 molecules EF
| #5: Protein | Mass: 8598.734 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
|---|---|
| #6: Protein/peptide | Mass: 3535.273 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein / Protein/peptide , 2 types, 2 molecules GX
| #16: Protein/peptide | Mass: 3056.640 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
|---|---|
| #7: Protein | Mass: 29196.828 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Sugars , 2 types, 4 molecules 


| #25: Sugar | | #26: Sugar | ChemComp-LMU / | |
|---|
-Non-polymers , 11 types, 65 molecules 




















| #18: Chemical | ChemComp-FE2 / | ||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| #19: Chemical | ChemComp-CLA / #20: Chemical | #21: Chemical | ChemComp-BCR / #22: Chemical | ChemComp-SQD / | #23: Chemical | ChemComp-LMG / #24: Chemical | ChemComp-LHG / #27: Chemical | ChemComp-BCT / | #28: Chemical | ChemComp-PL9 / | #29: Chemical | ChemComp-HEM / | #30: Water | ChemComp-HOH / | |
-Details
| Has ligand of interest | Y |
|---|---|
| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
|---|---|
| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-
Sample preparation
| Component | Name: TEF30-associated PSII core complex / Type: COMPLEX / Entity ID: #1-#17 / Source: NATURAL |
|---|---|
| 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 |
-
Electron microscopy imaging
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
|---|---|
| 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 / Nominal defocus max: 1800 nm / Nominal defocus min: 1300 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
-
Processing
| CTF correction | Type: PHASE FLIPPING ONLY |
|---|---|
| 3D reconstruction | Resolution: 2.98 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 45968 / Symmetry type: POINT |
Movie
Controller
About Yorodumi





China, 1items
Citation









PDBj











FIELD EMISSION GUN