+Open data
-Basic information
Entry | Database: PDB / ID: 6rhz | ||||||||||||
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Title | Structure of a minimal photosystem I from a green alga | ||||||||||||
Components |
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Keywords | PHOTOSYNTHESIS / photosystem I / green algae | ||||||||||||
Function / homology | Function and homology information photosynthesis, light harvesting / photosystem I / photosynthetic electron transport in photosystem I / photosystem I / photosystem II / chlorophyll binding / chloroplast thylakoid membrane / photosynthesis / 4 iron, 4 sulfur cluster binding / electron transfer activity ...photosynthesis, light harvesting / photosystem I / photosynthetic electron transport in photosystem I / photosystem I / photosystem II / chlorophyll binding / chloroplast thylakoid membrane / photosynthesis / 4 iron, 4 sulfur cluster binding / electron transfer activity / oxidoreductase activity / magnesium ion binding / metal ion binding Similarity search - Function | ||||||||||||
Biological species | Dunaliella salina (plant) | ||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å | ||||||||||||
Authors | Perez Boerema, A. / Klaiman, D. / Caspy, I. / Netzer-El, S.Y. / Amunts, A. / Nelson, N. | ||||||||||||
Funding support | Israel, Sweden, 3items
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Citation | Journal: Nat Plants / Year: 2020 Title: Structure of a minimal photosystem I from the green alga Dunaliella salina. Authors: Annemarie Perez-Boerema / Daniel Klaiman / Ido Caspy / Sigal Y Netzer-El / Alexey Amunts / Nathan Nelson / Abstract: Solar energy harnessed by oxygenic photosynthesis supports most of the life forms on Earth. In eukaryotes, photosynthesis occurs in chloroplasts and is achieved by membrane-embedded macromolecular ...Solar energy harnessed by oxygenic photosynthesis supports most of the life forms on Earth. In eukaryotes, photosynthesis occurs in chloroplasts and is achieved by membrane-embedded macromolecular complexes that contain core and peripheral antennae with multiple pigments. The structure of photosystem I (PSI) comprises the core and light-harvesting (LHCI) complexes, which together form PSI-LHCI. Here we determined the structure of PSI-LHCI from the salt-tolerant green alga Dunaliella salina using X-ray crystallography and electron cryo-microscopy. Our results reveal a previously undescribed configuration of the PSI core. It is composed of only 7 subunits, compared with 14-16 subunits in plants and the alga Chlamydomonas reinhardtii, and forms the smallest known PSI. The LHCI is poorly conserved at the sequence level and binds to pigments that form new energy pathways, and the interactions between the individual Lhca1-4 proteins are weakened. Overall, the data indicate the PSI of D. salina represents a different type of the molecular organization that provides important information for reconstructing the plasticity and evolution of PSI. | ||||||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 6rhz.cif.gz | 1.5 MB | Display | PDBx/mmCIF format |
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PDB format | pdb6rhz.ent.gz | 1.4 MB | Display | PDB format |
PDBx/mmJSON format | 6rhz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6rhz_validation.pdf.gz | 11.6 MB | Display | wwPDB validaton report |
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Full document | 6rhz_full_validation.pdf.gz | 12.1 MB | Display | |
Data in XML | 6rhz_validation.xml.gz | 175.5 KB | Display | |
Data in CIF | 6rhz_validation.cif.gz | 218.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rh/6rhz ftp://data.pdbj.org/pub/pdb/validation_reports/rh/6rhz | HTTPS FTP |
-Related structure data
Related structure data | 4883MC 6qphC C: citing same article (ref.) M: map data used to model this data |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-Chlorophyll a-b binding protein, ... , 4 types, 4 molecules 1234
#1: Protein | Mass: 21305.230 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) / References: UniProt: C1K003 |
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#2: Protein | Mass: 22813.822 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) |
#3: Protein | Mass: 22732.824 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) / References: UniProt: C1K004 |
#4: Protein | Mass: 23131.031 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) |
-Photosystem I P700 chlorophyll a apoprotein ... , 2 types, 2 molecules AB
#5: Protein | Mass: 81748.172 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) / References: UniProt: D0FXV2, photosystem I |
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#6: Protein | Mass: 81327.992 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) / References: UniProt: D0FXZ0, photosystem I |
-Photosystem I reaction center subunit ... , 4 types, 4 molecules DEFJ
#8: Protein | Mass: 15883.294 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) |
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#9: Protein | Mass: 7297.158 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) |
#10: Protein | Mass: 18212.902 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) |
#11: Protein/peptide | Mass: 4467.188 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) / References: UniProt: D0FXW0 |
-Protein / Sugars , 2 types, 2 molecules C
#22: Sugar | ChemComp-DGD / |
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#7: Protein | Mass: 8717.090 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) / References: UniProt: D0FXW7, photosystem I |
-Non-polymers , 10 types, 192 molecules
#12: Chemical | ChemComp-LUT / ( #13: Chemical | ChemComp-XAT / ( #14: Chemical | ChemComp-BCR / #15: Chemical | ChemComp-CLA / #16: Chemical | ChemComp-CHL / #17: Chemical | ChemComp-LHG / #18: Chemical | ChemComp-LMG / #19: Chemical | ChemComp-CL0 / | #20: Chemical | #21: Chemical | |
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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 / Type: COMPLEX / Entity ID: #1-#11 / Source: NATURAL | |||||||||||||||
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Molecular weight | Experimental value: NO | |||||||||||||||
Source (natural) | Organism: Dunaliella salina (plant) | |||||||||||||||
Buffer solution | pH: 8 | |||||||||||||||
Buffer component |
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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 | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K |
-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 |
Image recording | Electron dose: 41.6 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
Image scans | Movie frames/image: 40 |
-Processing
Software | Name: PHENIX / Version: 1.14_3260: / Classification: refinement | ||||||||||||||||||||||||
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EM software |
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CTF correction | Type: PHASE FLIPPING ONLY | ||||||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 132017 / Symmetry type: POINT | ||||||||||||||||||||||||
Atomic model building | Space: REAL | ||||||||||||||||||||||||
Atomic model building | PDB-ID: 5L8R | ||||||||||||||||||||||||
Refinement | Highest resolution: 3.2 Å / Stereochemistry target values: CDL v1.2 | ||||||||||||||||||||||||
Refine LS restraints |
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