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Yorodumi- PDB-10eg: Thermosynechococcus vestitus (BP-1) Photosystem I Complexed with ... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 10eg | ||||||||||||||||||||||||||||||
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| Title | Thermosynechococcus vestitus (BP-1) Photosystem I Complexed with Platinum Nanoparticles | ||||||||||||||||||||||||||||||
Components | (Photosystem I ...) x 12 | ||||||||||||||||||||||||||||||
Keywords | PHOTOSYNTHESIS / Nanoparticles / Biohybrid / Photosystem | ||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationphotosystem I reaction center / photosystem I / photosynthetic electron transport in photosystem I / photosystem I / plasma membrane-derived thylakoid membrane / chlorophyll binding / photosynthesis / 4 iron, 4 sulfur cluster binding / electron transfer activity / oxidoreductase activity ...photosystem I reaction center / photosystem I / photosynthetic electron transport in photosystem I / photosystem I / plasma membrane-derived thylakoid membrane / chlorophyll binding / photosynthesis / 4 iron, 4 sulfur cluster binding / electron transfer activity / oxidoreductase activity / magnesium ion binding / metal ion binding Similarity search - Function | ||||||||||||||||||||||||||||||
| Biological species | ![]() Thermosynechococcus vestitus BP-1 (bacteria) | ||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å | ||||||||||||||||||||||||||||||
Authors | Emerson, M.D. / Gisriel, C.J. | ||||||||||||||||||||||||||||||
| Funding support | United States, 1items
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Citation | Journal: bioRxiv / Year: 2026Title: Molecular design principles for Photosystem I-based biohybrid solar fuel catalysts. Authors: Maximino D Emerson / Siva Naga Sai Damaraju / Audrey H Short / Zachary B Alvord / Zsolt A Palmer / Himanshu S Mehra / Christian M Brininger / Josh V Vermaas / Lisa M Utschig / Christopher J Gisriel / ![]() Abstract: Direct solar-to-chemical conversion offers a compelling route to clean, dispatchable energy. Photosystem I (PSI), an evolutionarily optimized light-driven oxidoreductase central to oxygenic ...Direct solar-to-chemical conversion offers a compelling route to clean, dispatchable energy. Photosystem I (PSI), an evolutionarily optimized light-driven oxidoreductase central to oxygenic photosynthesis, can be repurposed for direct solar-fuel production by efficiently coupling its photochemistry to catalysts, thereby storing sunlight as chemical energy in the H-H bond of H2. One promising architecture integrates PSI with Pt nanoparticle (PtNP) catalysts to create photocatalytic PSI-PtNP biohybrids. Advancing these systems requires molecular-level insight into protein-nanoparticle interactions and the bio-nano electron transfer pathways that govern activity; however, progress has been constrained by limited structural data to guide rational design. Here, we present two molecular structures of active PSI-PtNP assemblies that (a) compare thermophilic and mesophilic PSI scaffolds and (b) probe how removal of the terminal [4Fe-4S] clusters and stromal subunits in PSI reshapes protein-nanoparticle interfaces and photocatalysis. Structural analyses and molecular dynamics simulations define the interface topology, electrostatics, and cofactor-to-nanoparticle distances, revealing key molecular features that control biohybrid formation and electron transfer efficiency. These data establish mechanistic links between scaffold composition, bio-nano interface geometry, and catalytic performance, yielding design principles for optimizing PSI-PtNP architectures. The resulting structure-function insights provide a blueprint for engineering PSI-based solar-fuels systems and, more broadly, inform the design of protein-nanomaterial interfaces for light-driven catalysis. | ||||||||||||||||||||||||||||||
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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 | 10eg.cif.gz | 1.7 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb10eg.ent.gz | 1.5 MB | Display | PDB format |
| PDBx/mmJSON format | 10eg.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/0e/10eg ftp://data.pdbj.org/pub/pdb/validation_reports/0e/10eg | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 75106MC 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
-Photosystem I ... , 12 types, 36 molecules AGaBHbCNcDOdEPeFQfIRiJSjKTkLUl...
| #1: Protein | Mass: 83267.773 Da / Num. of mol.: 3 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: P0A405, photosystem I #2: Protein | Mass: 83123.648 Da / Num. of mol.: 3 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: P0A407, photosystem I #3: Protein | Mass: 8809.207 Da / Num. of mol.: 3 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: P0A415, photosystem I #4: Protein | Mass: 15389.494 Da / Num. of mol.: 3 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: P0A420 #5: Protein | Mass: 8399.485 Da / Num. of mol.: 3 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: P0A423 #6: Protein | Mass: 17716.586 Da / Num. of mol.: 3 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: P0A401 #7: Protein/peptide | Mass: 4297.234 Da / Num. of mol.: 3 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: P0A427 #8: Protein/peptide | Mass: 4770.698 Da / Num. of mol.: 3 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: P0A429 #9: Protein | Mass: 8483.983 Da / Num. of mol.: 3 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: P0A425 #10: Protein | Mass: 16287.765 Da / Num. of mol.: 3 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: Q8DGB4 #11: Protein/peptide | Mass: 3426.115 Da / Num. of mol.: 3 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: P0A403 #12: Protein/peptide | Mass: 4424.317 Da / Num. of mol.: 3 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: Q8DKP6 |
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-Non-polymers , 8 types, 381 molecules 














| #13: Chemical | | #14: Chemical | ChemComp-CLA / #15: Chemical | ChemComp-PQN / #16: Chemical | ChemComp-BCR / #17: Chemical | ChemComp-LHG / #18: Chemical | ChemComp-SF4 / #19: Chemical | #20: Chemical | |
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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: Thermosynechococcus vestitus (BP-1) Photosystem I Complexed with Platinum Nanoparticles Type: COMPLEX / Entity ID: #1-#12 / Source: NATURAL |
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| Molecular weight | Value: 0.934541 MDa / Experimental value: NO |
| Source (natural) | Organism: ![]() Thermosynechococcus vestitus BP-1 (bacteria) |
| Buffer solution | pH: 7.4 |
| Buffer component | Conc.: 20 mM / Name: HEPES / Formula: C8H18N2O4S |
| 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: 277.5 K |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TALOS ARCTICA |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: OTHER / Nominal defocus max: 2200 nm / Nominal defocus min: 800 nm / C2 aperture diameter: 70 µm |
| Specimen holder | Cryogen: NITROGEN |
| Image recording | Average exposure time: 4.13 sec. / Electron dose: 1 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 3092 |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 906919 | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 19151 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 3.4 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
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About Yorodumi




Thermosynechococcus vestitus BP-1 (bacteria)
United States, 1items
Citation
PDBj












FIELD EMISSION GUN