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Yorodumi- PDB-8b11: cryo-EM structure of carboxysomal mini-shell: icosahedral assembl... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 8b11 | |||||||||
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| Title | cryo-EM structure of carboxysomal mini-shell: icosahedral assembly from CsoS4A/1A and CsoS2 co-expression (T = 4) | |||||||||
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Keywords | STRUCTURAL PROTEIN / carboxysome / shell / icosahedral symmetry | |||||||||
| Function / homology | Function and homology informationstructural constituent of carboxysome shell / carboxysome / carbon fixation Similarity search - Function | |||||||||
| Biological species | Halothiobacillus neapolitanus (bacteria) | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.52 Å | |||||||||
Authors | Ni, T. / Jiang, Q. / Liu, L.N. / Zhang, P. | |||||||||
| Funding support | United Kingdom, 2items
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Citation | Journal: Nat Commun / Year: 2023Title: Intrinsically disordered CsoS2 acts as a general molecular thread for α-carboxysome shell assembly. Authors: Tao Ni / Qiuyao Jiang / Pei Cing Ng / Juan Shen / Hao Dou / Yanan Zhu / Julika Radecke / Gregory F Dykes / Fang Huang / Lu-Ning Liu / Peijun Zhang / ![]() Abstract: Carboxysomes are a paradigm of self-assembling proteinaceous organelles found in nature, offering compartmentalisation of enzymes and pathways to enhance carbon fixation. In α-carboxysomes, the ...Carboxysomes are a paradigm of self-assembling proteinaceous organelles found in nature, offering compartmentalisation of enzymes and pathways to enhance carbon fixation. In α-carboxysomes, the disordered linker protein CsoS2 plays an essential role in carboxysome assembly and Rubisco encapsulation. Its mechanism of action, however, is not fully understood. Here we synthetically engineer α-carboxysome shells using minimal shell components and determine cryoEM structures of these to decipher the principle of shell assembly and encapsulation. The structures reveal that the intrinsically disordered CsoS2 C-terminus is well-structured and acts as a universal "molecular thread" stitching through multiple shell protein interfaces. We further uncover in CsoS2 a highly conserved repetitive key interaction motif, [IV]TG, which is critical to the shell assembly and architecture. Our study provides a general mechanism for the CsoS2-governed carboxysome shell assembly and cargo encapsulation and further advances synthetic engineering of carboxysomes for diverse biotechnological applications. | |||||||||
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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 | 8b11.cif.gz | 77.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8b11.ent.gz | 56.7 KB | Display | PDB format |
| PDBx/mmJSON format | 8b11.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8b11_validation.pdf.gz | 1.6 MB | Display | wwPDB validaton report |
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| Full document | 8b11_full_validation.pdf.gz | 1.6 MB | Display | |
| Data in XML | 8b11_validation.xml.gz | 35.7 KB | Display | |
| Data in CIF | 8b11_validation.cif.gz | 49.9 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b1/8b11 ftp://data.pdbj.org/pub/pdb/validation_reports/b1/8b11 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 15799MC ![]() 8b0yC ![]() 8b12C 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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| 1 | x 60![]()
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Components
| #1: Protein | Mass: 8900.287 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Halothiobacillus neapolitanus (bacteria)Strain: ATCC 23641 / c2 / Gene: csoS4A, orfA, Hneap_0918 / Production host: ![]() | ||
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| #2: Protein | Mass: 9973.478 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Halothiobacillus neapolitanus (bacteria)Strain: ATCC 23641 / c2 / Gene: csoS1A, csoS1, Hneap_0915 / Production host: ![]() #3: Water | ChemComp-HOH / | |
-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: mini-shell assembly from Halothiobacillus neapolitanus with CsoS4A/1A and CsoS2 co-expression (T= 4) Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT |
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| Source (natural) | Organism: Halothiobacillus neapolitanus (bacteria) |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 8 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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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: 1000 nm |
| Image recording | Electron dose: 44 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||
| Symmetry | Point symmetry: I (icosahedral) | ||||||||||||||||||
| 3D reconstruction | Resolution: 2.52 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 13515 / Algorithm: FOURIER SPACE / Symmetry type: POINT | ||||||||||||||||||
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About Yorodumi



Halothiobacillus neapolitanus (bacteria)
United Kingdom, 2items
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FIELD EMISSION GUN

