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Yorodumi- PDB-21wv: In situ structure of the C2S2M2L4-type PSII-LHCII supercomplex fr... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 21wv | |||||||||
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| Title | In situ structure of the C2S2M2L4-type PSII-LHCII supercomplex from Oryza sativa | |||||||||
Components |
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Keywords | PHOTOSYNTHESIS / Photosystem II / C2S2M2L4-type / in situ / Oryza sativa / Chloroplast | |||||||||
| Function / homology | Function and homology informationchloroplast photosystem II / photosynthesis, light harvesting in photosystem I / chloroplast thylakoid / photosystem II oxygen evolving complex / photosystem II assembly / photosynthesis, light harvesting / thylakoid / oxygen evolving activity / photosystem II stabilization / photosystem II reaction center ...chloroplast photosystem II / photosynthesis, light harvesting in photosystem I / chloroplast thylakoid / photosystem II oxygen evolving complex / photosystem II assembly / photosynthesis, light harvesting / thylakoid / oxygen evolving activity / photosystem II stabilization / photosystem II reaction center / photosystem II / photosystem I / photosynthetic electron transport chain / photosystem II / extrinsic component of membrane / chlorophyll binding / plastid / photosynthetic electron transport in photosystem II / photosynthesis, light reaction / phosphate ion binding / chloroplast thylakoid membrane / response to light stimulus / photosynthesis / manganese ion binding / electron transfer activity / protein stabilization / iron ion binding / mRNA binding / heme binding / calcium ion binding / metal ion binding Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.89 Å | |||||||||
Authors | Li, J. / Elias, E. / Zhang, K. / Croce, R. / Zhu, J. | |||||||||
| Funding support | China, 1items
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Citation | Journal: Nature / Year: 2026Title: In situ structures of plant photosystem supercomplexes. Authors: Jiao Li / Eduard Elias / Kai Zhang / Roberta Croce / Jiapeng Zhu / ![]() Abstract: Photosynthesis sustains life on Earth by converting light to chemical energy through the coordinated action of photosystem I (PSI) and photosystem II (PSII) within thylakoid membranes. Although ...Photosynthesis sustains life on Earth by converting light to chemical energy through the coordinated action of photosystem I (PSI) and photosystem II (PSII) within thylakoid membranes. Although structures of isolated photosystems are available, their native organization in chloroplasts remains unknown. Here, using in situ cryo-electron microscopy, we directly imaged Oryza sativa (rice) chloroplasts and determined structures of photosystem supercomplexes in their native membrane environment. We resolved a CSML-type PSII-light harvesting complex II (LHCII) supercomplex, including four LHCII antenna trimers that were not retained in purified preparations. Excitation energy transfer calculations based on this architecture closely reproduce in vivo measurements, indicating its physiological relevance. We also resolved asymmetric PSII-LHCII dimers, including side-by-side, trans-lumenal and trans-stromal architectures, and higher-order assemblies of trimers and tetramers. On the basis of these observations, we propose that PSII forms a trans-lumenal and trans-stromal 'skeleton' that shapes thylakoid morphology and supports grana stacking. In addition, we obtained high-resolution structures of PSI-LHCI-LHCII and PSI-LHCI supercomplexes. Together, these structures reveal extensive networks of lipids, pigments and cofactors, providing the first molecular framework for understanding how the native architecture of plant photosystem supports the exceptional photon-to-electron efficiency of photosynthesis. | |||||||||
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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 | 21wv.cif.gz | 2.4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb21wv.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 21wv.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/1w/21wv ftp://data.pdbj.org/pub/pdb/validation_reports/1w/21wv | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 68060MC ![]() 21wdC ![]() 21wgC ![]() 21whC ![]() 21wiC ![]() 27urC ![]() 27utC ![]() 9xj1C ![]() 9xj9C ![]() 9xk3C ![]() 9xk4C ![]() 9xk6C ![]() 9xk7C ![]() 9xk8C ![]() 9xk9C 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
-Chlorophyll a-b binding protein ... , 2 types, 18 molecules 0001020506091114171G1N1g1n2013161922
| #1: Protein | Mass: 23441.461 Da / Num. of mol.: 14 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P12331 #5: Protein | Mass: 23368.408 Da / Num. of mol.: 4 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P12330 |
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-Protein , 3 types, 6 molecules 03071O1o1P1p
| #2: Protein | Mass: 24065.338 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: B7E6H8 #18: Protein | Mass: 26609.848 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q943W1 #19: Protein | Mass: 20122.322 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q8GTK4 |
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-Chlorophyll a-b binding protein, ... , 4 types, 10 molecules 0408121518211R1r1S1s
| #3: Protein | Mass: 22550.580 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q7XV11 #4: Protein | Mass: 24045.150 Da / Num. of mol.: 4 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q10HD0 #20: Protein | Mass: 25938.283 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q6Z411 #21: Protein | Mass: 23719.938 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q53N83 |
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-Photosystem II ... , 14 types, 28 molecules 1A1a1B1b1C1c1D1d1H1h1I1i1J1j1K1k1L1l1M1m1T1t1V1v1W1w1Z1z
| #6: Protein | Mass: 36917.039 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P0C432, photosystem II #7: Protein | Mass: 55632.102 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P0C362 #8: Protein | Mass: 49289.438 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P0C365 #9: Protein | Mass: 38268.645 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P0C435, photosystem II #12: Protein | Mass: 6472.638 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P0C420 #13: Protein/peptide | Mass: 3912.664 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P0C405 #14: Protein/peptide | Mass: 3586.210 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P0C414 #15: Protein/peptide | Mass: 4273.128 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P0C408 #16: Protein/peptide | Mass: 4265.800 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P60137 #17: Protein/peptide | Mass: 3668.451 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P0C411 #22: Protein/peptide | Mass: 3692.472 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P0C427 #24: Protein | Mass: 10861.420 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q8H4P7 #25: Protein | Mass: 5866.499 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q5ZBY9 #28: Protein | Mass: 6582.766 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P0C429 |
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-Cytochrome b559 subunit ... , 2 types, 4 molecules 1E1e1F1f
| #10: Protein | Mass: 8654.690 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P0C368 #11: Protein/peptide | Mass: 4027.779 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P0C401 |
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-Protein/peptide , 3 types, 6 molecules 1U1u1X1x1Y1y
| #23: Protein/peptide | Mass: 3009.631 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q0E032 #26: Protein/peptide | Mass: 3927.654 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q7EXX2 #27: Protein/peptide | Mass: 4061.776 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q6ZJ41 |
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-Sugars , 1 types, 13 molecules 
| #34: Sugar | ChemComp-DGD / |
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-Non-polymers , 18 types, 479 molecules 


































| #29: Chemical | ChemComp-CLA / #30: Chemical | ChemComp-CHL / #31: Chemical | ChemComp-LUT / ( #32: Chemical | #33: Chemical | ChemComp-LHG / #35: Chemical | ChemComp-BCR / #36: Chemical | #37: Chemical | ChemComp-CL / #38: Chemical | ChemComp-PHO / #39: Chemical | #40: Chemical | ChemComp-PL9 / #41: Chemical | ChemComp-SQD / #42: Chemical | ChemComp-MGE / ( #43: Chemical | #44: Chemical | #45: Chemical | #46: Chemical | ChemComp-XAT / ( #47: Chemical | ChemComp-3PH / | |
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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: Chloroplast / Type: COMPLEX / Entity ID: #1-#28 / Source: NATURAL |
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| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.3 |
| 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: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2200 nm / Nominal defocus min: 1400 nm |
| Image recording | Electron dose: 1.375 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.89 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 172752 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 2.89 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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