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Open data
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Basic information
Entry | Database: PDB / ID: 6tcl | ||||||||||||||||||
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Title | Photosystem I tetramer | ||||||||||||||||||
![]() | (Photosystem I ...) x 18 | ||||||||||||||||||
![]() | PHOTOSYNTHESIS / tetramer / anabaena / PSI | ||||||||||||||||||
Function / homology | ![]() photosystem I reaction center / photosystem I / photosynthetic electron transport in photosystem I / photosystem I / chlorophyll binding / plasma membrane-derived thylakoid membrane / photosynthesis / 4 iron, 4 sulfur cluster binding / oxidoreductase activity / electron transfer activity ...photosystem I reaction center / photosystem I / photosynthetic electron transport in photosystem I / photosystem I / chlorophyll binding / plasma membrane-derived thylakoid membrane / photosynthesis / 4 iron, 4 sulfur cluster binding / oxidoreductase activity / electron transfer activity / magnesium ion binding / metal ion binding Similarity search - Function | ||||||||||||||||||
Biological species | ![]() | ||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å | ||||||||||||||||||
![]() | Chen, M. / Perez-Boerema, A. / Li, S. / Amunts, A. | ||||||||||||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Distinct structural modulation of photosystem I and lipid environment stabilizes its tetrameric assembly. Authors: Ming Chen / Annemarie Perez-Boerema / Laixing Zhang / Yanxue Li / Maojun Yang / Shizhong Li / Alexey Amunts / ![]() ![]() Abstract: Photosystem I (PSI) is able to form different oligomeric states across various species. To reveal the structural basis for PSI dimerization and tetramerization, we structurally investigated PSI from ...Photosystem I (PSI) is able to form different oligomeric states across various species. To reveal the structural basis for PSI dimerization and tetramerization, we structurally investigated PSI from the cyanobacterium Anabaena. This revealed a disrupted trimerization domain due to lack of the terminal residues of PsaL in the lumen, which resulted in PSI dimers with loose connections between monomers and weaker energy-coupled chlorophylls than in the trimer. At the dimer surface, specific phospholipids, cofactors and interactions in combination facilitated recruitment of another dimer to form a tetramer. Taken together, the relaxed luminal connections and lipid specificity at the dimer interface account for membrane curvature. PSI tetramer assembly appears to increase the surface area of the thylakoid membrane, which would contribute to PSI crowding. | ||||||||||||||||||
History |
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 4.8 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 23.9 MB | Display | ![]() |
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Full document | ![]() | 25.1 MB | Display | |
Data in XML | ![]() | 467.8 KB | Display | |
Data in CIF | ![]() | 575.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 10461MC 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 ... , 18 types, 48 molecules A1A2AAAB1B2BBBC1C2CCCD1D2DDDE1E2F1FFFI1IIIJ1J2JJJK1K...
#1: Protein | Mass: 81932.125 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Protein | Mass: 83254.734 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Protein | Mass: 8694.010 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | Mass: 14672.670 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | Mass: 6809.673 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | Mass: 15030.004 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #7: Protein/peptide | Mass: 3550.169 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #8: Protein/peptide | Mass: 5368.227 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein | Mass: 7580.861 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #10: Protein | | Mass: 17545.008 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #11: Protein/peptide | Mass: 3407.008 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein/peptide | Mass: 4342.132 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #13: Protein | | Mass: 14845.810 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #14: Protein/peptide | | Mass: 3764.388 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #15: Protein | | Mass: 7509.784 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #16: Protein | | Mass: 17673.137 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #17: Protein | Mass: 7106.979 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #18: Protein | Mass: 16290.655 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Sugars , 1 types, 2 molecules 
#28: Sugar |
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-Non-polymers , 9 types, 576 molecules 
















#19: Chemical | ChemComp-CLA / #20: Chemical | ChemComp-CL0 / #21: Chemical | ChemComp-PQN / #22: Chemical | ChemComp-LHG / #23: Chemical | ChemComp-BCR / #24: Chemical | ChemComp-AJP / #25: Chemical | ChemComp-LMG / #26: Chemical | ChemComp-ECH / #27: Chemical | ChemComp-SF4 / |
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-Details
Has ligand of interest | Y |
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-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: Photosystem I / Type: COMPLEX / Entity ID: #1-#18 / Source: NATURAL |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: ![]() |
Buffer solution | pH: 6.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 |
Vitrification | Cryogen name: ETHANE / Humidity: 100 % |
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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: ![]() |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 42 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
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EM software |
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CTF correction | Type: PHASE FLIPPING ONLY | ||||||||||||||||||||||||
Particle selection | Num. of particles selected: 428587 | ||||||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 69247 / Symmetry type: POINT | ||||||||||||||||||||||||
Refinement | Stereochemistry target values: CDL v1.2 | ||||||||||||||||||||||||
Refine LS restraints |
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