+Open data
-Basic information
Entry | Database: PDB / ID: 6sl5 | |||||||||
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Title | Dunaliella Photosystem I Supercomplex | |||||||||
Components |
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Keywords | PHOTOSYNTHESIS / membrane complex / photosystem I / dunaliella / light harvesting / excitation transfer | |||||||||
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: 2.84 Å | |||||||||
Authors | Nelson, N. / Caspy, I. / Malavath, T. / Klaiman, D. / Shkolinsky, Y. | |||||||||
Funding support | Israel, Belgium, 2items
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Citation | Journal: Biochim Biophys Acta Bioenerg / Year: 2020 Title: Structure and energy transfer pathways of the Dunaliella Salina photosystem I supercomplex. Authors: Ido Caspy / Tirupathi Malavath / Daniel Klaiman / Maria Fadeeva / Yoel Shkolnisky / Nathan Nelson / Abstract: Oxygenic photosynthesis evolved more than 3 billion years ago in cyanobacteria. The increased complexity of photosystem I (PSI) became apparent from the high-resolution structures that were obtained ...Oxygenic photosynthesis evolved more than 3 billion years ago in cyanobacteria. The increased complexity of photosystem I (PSI) became apparent from the high-resolution structures that were obtained for the complexes that were isolated from various organisms, ranging from cyanobacteria to plants. These complexes are all evolutionarily linked. In this paper, the researchers have uncovered the increased complexity of PSI in a single organism demonstrated by the coexistance of two distinct PSI compositions. The Large Dunaliella PSI contains eight additional subunits, six in PSI core and two light harvesting complexes. Two additional chlorophyll a molecules pertinent for efficient excitation energy transfer in state II transition were identified in PsaL and PsaO. Short distances between these newly identified chlorophylls correspond with fast excitation transfer rates previously reported during state II transition. The apparent PSI conformations could be a coping mechanism for the high salinity. | |||||||||
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 | 6sl5.cif.gz | 1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb6sl5.ent.gz | 867.3 KB | Display | PDB format |
PDBx/mmJSON format | 6sl5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6sl5_validation.pdf.gz | 16.9 MB | Display | wwPDB validaton report |
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Full document | 6sl5_full_validation.pdf.gz | 17.8 MB | Display | |
Data in XML | 6sl5_validation.xml.gz | 304.7 KB | Display | |
Data in CIF | 6sl5_validation.cif.gz | 358 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sl/6sl5 ftp://data.pdbj.org/pub/pdb/validation_reports/sl/6sl5 | HTTPS FTP |
-Related structure data
Related structure data | 10236MC 6yxrC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-Photosystem I ... , 4 types, 4 molecules ABCJ
#1: Protein | Mass: 81877.352 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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#2: Protein | Mass: 81671.438 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) / References: UniProt: D0FXZ0, photosystem I |
#3: 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 |
#7: Protein/peptide | Mass: 4614.362 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) / References: UniProt: D0FXW0 |
-Protein , 12 types, 12 molecules DEFGHKLO2456
#4: Protein | Mass: 16214.705 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) |
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#5: Protein | Mass: 7297.158 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) |
#6: Protein | Mass: 18115.789 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) |
#8: Protein | Mass: 10928.419 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) |
#9: Protein | Mass: 10012.247 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) |
#11: Protein | Mass: 8191.218 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) |
#12: Protein | Mass: 16189.839 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) |
#13: Protein | Mass: 9635.004 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) |
#15: Protein | Mass: 22813.822 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) |
#17: Protein | Mass: 23131.031 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) |
#18: Protein | Mass: 21676.771 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) |
#19: Protein | Mass: 19559.611 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) |
-Protein/peptide , 1 types, 1 molecules I
#10: Protein/peptide | Mass: 4236.944 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) |
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-Chlorophyll a-b binding protein, ... , 2 types, 2 molecules 13
#14: 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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#16: Protein | Mass: 24585.910 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Dunaliella salina (plant) / References: UniProt: C1K004*PLUS |
-Sugars , 2 types, 8 molecules
#27: Sugar | ChemComp-LMU / #28: Sugar | ChemComp-DGD / |
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-Non-polymers , 18 types, 284 molecules
#20: Chemical | ChemComp-CL0 / | ||||||||||||||||||||||||||||||||
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#21: Chemical | ChemComp-CLA / #22: Chemical | #23: Chemical | #24: Chemical | ChemComp-BCR / #25: Chemical | ChemComp-LHG / #26: Chemical | ChemComp-OCD / | #29: Chemical | ChemComp-3PH / #30: Chemical | ChemComp-CA / | #31: Chemical | ChemComp-LMG / #32: Chemical | #33: Chemical | ChemComp-PTY / #34: Chemical | ChemComp-LUT / ( #35: Chemical | ChemComp-XAT / ( #36: Chemical | ChemComp-CHL / #37: Chemical | #38: Chemical | #39: Chemical | |
-Details
Has ligand of interest | N |
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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: Large dunaliella salina photosystem I-LHC supercomplex Type: COMPLEX / Entity ID: #1-#19 / Source: NATURAL |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: Dunaliella salina (plant) |
Buffer solution | pH: 8 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid material: COPPER / Grid type: Quantifoil R1.2/1.3 |
Vitrification | Instrument: LEICA EM GP / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K / Details: 2.5 sec blotting before plunging |
-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 / Nominal defocus max: 3000 nm / Nominal defocus min: 900 nm |
Image recording | Electron dose: 42.68 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 4306 |
-Processing
Software |
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EM software |
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CTF correction | Type: NONE | ||||||||||||||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 720711 | ||||||||||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 2.84 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 189006 / Num. of class averages: 2 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||
Atomic model building | B value: 83 / Protocol: AB INITIO MODEL / Space: REAL | ||||||||||||||||||||||||||||||||||||||||
Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 1.34 Å2 | ||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
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