+Open data
-Basic information
Entry | Database: PDB / ID: 8htu | ||||||
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Title | Cryo-EM structure of PpPSI-L | ||||||
Components |
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Keywords | PHOTOSYNTHESIS / Lhcb9 / PSI | ||||||
Function / homology | Function and homology information photosynthesis, light harvesting in photosystem I / chloroplast thylakoid lumen / photosynthesis, light harvesting / photosystem I reaction center / photosystem I / photosynthetic electron transport in photosystem I / photosystem I / photosystem II / chlorophyll binding / chloroplast thylakoid membrane ...photosynthesis, light harvesting in photosystem I / chloroplast thylakoid lumen / photosynthesis, light harvesting / 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 / magnesium ion binding / membrane / metal ion binding Similarity search - Function | ||||||
Biological species | Physcomitrium patens (plant) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.87 Å | ||||||
Authors | Li, M. / Pan, X.W. / Sun, H.Y. | ||||||
Funding support | China, 1items
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Citation | Journal: Nat Plants / Year: 2023 Title: Structural insights into the assembly and energy transfer of the Lhcb9-dependent photosystem I from moss Physcomitrium patens. Authors: Haiyu Sun / Hui Shang / Xiaowei Pan / Mei Li / Abstract: In plants and green algae, light-harvesting complexes I and II (LHCI and LHCII) constitute the antennae of photosystem I (PSI), thus effectively increasing the cross-section of the PSI core. The moss ...In plants and green algae, light-harvesting complexes I and II (LHCI and LHCII) constitute the antennae of photosystem I (PSI), thus effectively increasing the cross-section of the PSI core. The moss Physcomitrium patens (P. patens) represents a well-studied primary land-dwelling photosynthetic autotroph branching from the common ancestor of green algae and land plants at the early stage of evolution. P. patens possesses at least three types of PSI with different antenna sizes. The largest PSI form (PpPSI-L) exhibits a unique organization found neither in flowering plants nor in algae. Its formation is mediated by the P. patens-specific LHC protein, Lhcb9. While previous studies have revealed the overall architecture of PpPSI-L, its assembly details and the relationship between different PpPSI types remain unclear. Here we report the high-resolution structure of PpPSI-L. We identified 14 PSI core subunits, one Lhcb9, one phosphorylated LHCII trimer and eight LHCI monomers arranged as two belts. Our structural analysis established the essential role of Lhcb9 and the phosphorylated LHCII in stabilizing the complex. In addition, our results suggest that PpPSI switches between different types, which share identical modules. This feature may contribute to the dynamic adjustment of the light-harvesting capability of PSI under different light conditions. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8htu.cif.gz | 1.3 MB | Display | PDBx/mmCIF format |
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PDB format | pdb8htu.ent.gz | 1.1 MB | Display | PDB format |
PDBx/mmJSON format | 8htu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ht/8htu ftp://data.pdbj.org/pub/pdb/validation_reports/ht/8htu | HTTPS FTP |
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-Related structure data
Related structure data | 35018MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-Chlorophyll a-b binding protein, ... , 6 types, 12 molecules UVW152637489
#1: Protein | Mass: 28403.947 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Physcomitrium patens (plant) / References: UniProt: A9RT62 #2: Protein | Mass: 25931.562 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Physcomitrium patens (plant) / References: UniProt: A0A2K1JLZ3 #3: Protein | Mass: 29036.998 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Physcomitrium patens (plant) / References: UniProt: A9TJ06 #4: Protein | Mass: 34673.801 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Physcomitrium patens (plant) / References: UniProt: A0A2K1IB10 #5: Protein | Mass: 28818.881 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Physcomitrium patens (plant) / References: UniProt: A0A2K1K0E4 #20: Protein | | Mass: 33175.734 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Physcomitrium patens (plant) / References: UniProt: A0A2K1KKR9 |
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-Photosystem I P700 chlorophyll a apoprotein ... , 2 types, 2 molecules AB
#6: Protein | Mass: 83226.508 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Physcomitrium patens (plant) / References: UniProt: Q8MFA3, photosystem I |
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#7: Protein | Mass: 82447.750 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Physcomitrium patens (plant) / References: UniProt: Q8MFA2, photosystem I |
-Protein , 2 types, 2 molecules CL
#8: Protein | Mass: 8781.153 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Physcomitrium patens (plant) / References: UniProt: Q6YXQ2, photosystem I |
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#17: Protein | Mass: 23530.299 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Physcomitrium patens (plant) / References: UniProt: A0A7I4A0Q6 |
-Photosystem I reaction center subunit ... , 8 types, 8 molecules DEFGHIJM
#9: Protein | Mass: 22183.309 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Physcomitrium patens (plant) / References: UniProt: A9REG3 |
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#10: Protein | Mass: 13919.796 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Physcomitrium patens (plant) / References: UniProt: A0A2K1IHL7 |
#11: Protein | Mass: 26112.318 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Physcomitrium patens (plant) / References: UniProt: A0A2K1IN36 |
#12: Protein | Mass: 16231.396 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Physcomitrium patens (plant) / References: UniProt: A0A2K1JC42 |
#13: Protein | Mass: 14506.459 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Physcomitrium patens (plant) / References: UniProt: A0A2K1JDR4 |
#14: Protein/peptide | Mass: 4017.787 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Physcomitrium patens (plant) / References: UniProt: Q6YXR3 |
#15: Protein/peptide | Mass: 4597.460 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Physcomitrium patens (plant) / References: UniProt: Q6YXM2 |
#18: Protein/peptide | Mass: 3412.051 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Physcomitrium patens (plant) / References: UniProt: Q6YXK4 |
-Photosystem I subunit ... , 2 types, 2 molecules KO
#16: Protein | Mass: 13278.444 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Physcomitrium patens (plant) / References: UniProt: A0A2K1KU02 |
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#19: Protein | Mass: 15393.113 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Physcomitrium patens (plant) / References: UniProt: A0A2K1JDF1 |
-Sugars , 2 types, 5 molecules
#31: Sugar | ChemComp-LMT / #32: Sugar | ChemComp-DGD / | |
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-Non-polymers , 11 types, 363 molecules
#21: Chemical | ChemComp-CHL / #22: Chemical | ChemComp-CLA / #23: Chemical | ChemComp-LUT / ( #24: Chemical | ChemComp-XAT / ( #25: Chemical | ChemComp-NEX / ( #26: Chemical | ChemComp-LHG / #27: Chemical | ChemComp-BCR / #28: Chemical | ChemComp-LMG / #29: Chemical | #30: Chemical | #33: Water | ChemComp-HOH / | |
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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 |
-Sample preparation
Component | Name: photosystem I from Physcomitrium patens / Type: COMPLEX / Entity ID: #1-#20 / Source: NATURAL |
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Source (natural) | Organism: Physcomitrium patens (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: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: OTHER / Accelerating voltage: 300 kV / Illumination mode: OTHER |
Electron lens | Mode: OTHER / Nominal defocus max: 2500 nm / Nominal defocus min: 1500 nm |
Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
-Processing
EM software | Name: PHENIX / Version: 1.19.2_4158: / Category: model refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 2.87 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 144586 / Symmetry type: POINT | ||||||||||||||||||||||||
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