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Yorodumi- PDB-9m3j: structure of bundle-shaped PBS with both long rod and (ApcA2B3Apc... -
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Basic information
| Entry | Database: PDB / ID: 9m3j | ||||||||||||||||||||||||
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| Title | structure of bundle-shaped PBS with both long rod and (ApcA2B3ApcD) trimer | ||||||||||||||||||||||||
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Keywords | PHOTOSYNTHESIS / phycobilisome / light-harvesting complex | ||||||||||||||||||||||||
| Function / homology | Function and homology informationphycobilisome / plasma membrane-derived thylakoid membrane / photosynthesis / lyase activity Similarity search - Function | ||||||||||||||||||||||||
| Biological species | Gloeobacter violaceus PCC 7421 (bacteria) | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.37 Å | ||||||||||||||||||||||||
Authors | Ma, J. / Sui, S.-F. | ||||||||||||||||||||||||
| Funding support | China, 2items
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Citation | Journal: Nat Commun / Year: 2025Title: Light-induced structural adaptation of the bundle-shaped phycobilisome from thylakoid-lacking cyanobacterium Gloeobacter violaceus. Authors: Jianfei Ma / Xin You / Shan Sun / Sen-Fang Sui / ![]() Abstract: Gloeobacter diverged from other lineages early in cyanobacterial evolution, preferentially growing under low light intensity conditions. Among cyanobacteria, G. violaceus exhibits unique features, ...Gloeobacter diverged from other lineages early in cyanobacterial evolution, preferentially growing under low light intensity conditions. Among cyanobacteria, G. violaceus exhibits unique features, including lack of a thylakoid membrane and bundle-shaped antenna phycobilisomes (PBSs), densely packed and well-organized on the plasma membrane. However, without high-resolution structures, it has remained unclear how G. violaceus PBSs assemble into a bundle-shaped configuration. Here we solve the cryo-EM structures of PBSs from G. violaceus cells cultured under low (Sr-PBS) or moderate (Lr-PBS) light intensity. These structures reveal two unique linker proteins, L and L, that play a key role in the PBS architecture. Analysis of the bilin arrangement indicates that the bundle-shaped structure allows efficient energy transfer among rods. Moreover, comparison between Lr-PBS and Sr-PBS uncovers a distinct mode of adaption to increased light intensity wherein the ApcA-ApcB-ApcD layer can be blocked from binding to the core by altering structural elements exclusively found in the G. violaceus L. This study illustrates previously unrecognized mechanisms of assembly and adaptation to varying light intensity in the bundle-shaped PBS of G. violaceus. | ||||||||||||||||||||||||
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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 | 9m3j.cif.gz | 3.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9m3j.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9m3j.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9m3j_validation.pdf.gz | 7.3 MB | Display | wwPDB validaton report |
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| Full document | 9m3j_full_validation.pdf.gz | 8 MB | Display | |
| Data in XML | 9m3j_validation.xml.gz | 519.3 KB | Display | |
| Data in CIF | 9m3j_validation.cif.gz | 767.7 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m3/9m3j ftp://data.pdbj.org/pub/pdb/validation_reports/m3/9m3j | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 63604MC ![]() 9k9wC C: citing same article ( M: map data used to model this data |
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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
-Allophycocyanin ... , 2 types, 92 molecules A1C1E1H1A2C2E2G2I2K2M2O2Q2S2U2W2Y2a2c2e2g2i2k2m2o2q2s2u2A3C3...
| #1: Protein | Mass: 17539.039 Da / Num. of mol.: 44 / Source method: isolated from a natural source / Source: (natural) Gloeobacter violaceus PCC 7421 (bacteria)#2: Protein | Mass: 17241.664 Da / Num. of mol.: 48 / Source method: isolated from a natural source / Source: (natural) Gloeobacter violaceus PCC 7421 (bacteria) / References: UniProt: Q7NL79 |
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-Protein , 3 types, 12 molecules K1L1z1M1z2w2x2y2z3i3j3k3
| #3: Protein | Mass: 18050.812 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Gloeobacter violaceus PCC 7421 (bacteria)#4: Protein | Mass: 7765.004 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Source: (natural) Gloeobacter violaceus PCC 7421 (bacteria) / References: UniProt: Q7NL78#5: Protein | Mass: 130002.258 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Gloeobacter violaceus PCC 7421 (bacteria) / References: UniProt: Q7NL81 |
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-Non-polymers , 1 types, 96 molecules 
| #6: Chemical | ChemComp-CYC / |
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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: phycobilisome / Type: COMPLEX / Entity ID: #1-#5 / Source: NATURAL | |||||||||||||||
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| Molecular weight | Value: 7 MDa / Experimental value: YES | |||||||||||||||
| Source (natural) | Organism: Gloeobacter violaceus PCC 7421 (bacteria) / Strain: PCC 7421 | |||||||||||||||
| Buffer solution | pH: 7 | |||||||||||||||
| Buffer component |
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| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | |||||||||||||||
| Specimen support | Grid type: Quantifoil R2/1 | |||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 18 K |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Tecnai F30 / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TECNAI F30 |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 64000 X / Calibrated magnification: 64000 X / Nominal defocus max: 2300 nm / Nominal defocus min: 1300 nm / Calibrated defocus min: 1300 nm / Calibrated defocus max: 2300 nm / Cs: 0.001 mm / C2 aperture diameter: 100 µm / Alignment procedure: COMA FREE |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Temperature (max): 77 K / Temperature (min): 77 K |
| Image recording | Average exposure time: 8.2 sec. / Electron dose: 50 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 2 / Num. of real images: 10942 |
| EM imaging optics | Energyfilter name: GIF Quantum ER / Energyfilter slit width: 20 eV Spherical aberration corrector: Spherical aberration (Cs) corrector |
| Image scans | Width: 5760 / Height: 4092 / Movie frames/image: 32 / Used frames/image: 1-32 |
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Processing
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| CTF correction | Type: NONE | ||||||||||||||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 605750 | ||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.37 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 192814 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||
| Atomic model building | B value: 62.05 / Protocol: RIGID BODY FIT / Space: REAL / Target criteria: 0,99 | ||||||||||||||||||||||||||||||||||||
| Atomic model building | Source name: AlphaFold / Type: in silico model |
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About Yorodumi



Gloeobacter violaceus PCC 7421 (bacteria)
China, 2items
Citation



PDBj

FIELD EMISSION GUN