+Open data
-Basic information
Entry | Database: PDB / ID: 7zc1 | ||||||||||||
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Title | Subtomogram averaging of Rubisco from Cyanobium carboxysome | ||||||||||||
Components |
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Keywords | UNKNOWN FUNCTION / Rubisco / alpha carboxysomes | ||||||||||||
Function / homology | Function and homology information carboxysome / photorespiration / ribulose-bisphosphate carboxylase / ribulose-bisphosphate carboxylase activity / reductive pentose-phosphate cycle / monooxygenase activity / magnesium ion binding Similarity search - Function | ||||||||||||
Biological species | Cyanobium sp. PCC 7001 (bacteria) | ||||||||||||
Method | ELECTRON MICROSCOPY / subtomogram averaging / cryo EM / Resolution: 3.8 Å | ||||||||||||
Authors | Ni, T. / Zhu, Y. / Seaton-Burn, W. / Zhang, P. | ||||||||||||
Funding support | United Kingdom, European Union, 3items
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Citation | Journal: Nat Commun / Year: 2022 Title: Structure and assembly of cargo Rubisco in two native α-carboxysomes. Authors: Tao Ni / Yaqi Sun / Will Burn / Monsour M J Al-Hazeem / Yanan Zhu / Xiulian Yu / Lu-Ning Liu / Peijun Zhang / Abstract: Carboxysomes are a family of bacterial microcompartments in cyanobacteria and chemoautotrophs. They encapsulate Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) and carbonic anhydrase ...Carboxysomes are a family of bacterial microcompartments in cyanobacteria and chemoautotrophs. They encapsulate Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) and carbonic anhydrase catalyzing carbon fixation inside a proteinaceous shell. How Rubisco complexes pack within the carboxysomes is unknown. Using cryo-electron tomography, we determine the distinct 3D organization of Rubisco inside two distant α-carboxysomes from a marine α-cyanobacterium Cyanobium sp. PCC 7001 where Rubiscos are organized in three concentric layers, and from a chemoautotrophic bacterium Halothiobacillus neapolitanus where they form intertwining spirals. We further resolve the structures of native Rubisco as well as its higher-order assembly at near-atomic resolutions by subtomogram averaging. The structures surprisingly reveal that the authentic intrinsically disordered linker protein CsoS2 interacts with Rubiscos in native carboxysomes but functions distinctively in the two α-carboxysomes. In contrast to the uniform Rubisco-CsoS2 association in the Cyanobium α-carboxysome, CsoS2 binds only to the Rubiscos close to the shell in the Halo α-carboxysome. Our findings provide critical knowledge of the assembly principles of α-carboxysomes, which may aid in the rational design and repurposing of carboxysome structures for new functions. | ||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7zc1.cif.gz | 732.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7zc1.ent.gz | 618.1 KB | Display | PDB format |
PDBx/mmJSON format | 7zc1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7zc1_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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Full document | 7zc1_full_validation.pdf.gz | 1.5 MB | Display | |
Data in XML | 7zc1_validation.xml.gz | 124.2 KB | Display | |
Data in CIF | 7zc1_validation.cif.gz | 186.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zc/7zc1 ftp://data.pdbj.org/pub/pdb/validation_reports/zc/7zc1 | HTTPS FTP |
-Related structure data
Related structure data | 14617MC 7zbtC C: citing same article (ref.) M: map data used to model this data |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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-Components
#1: Protein | Mass: 52526.531 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Cyanobium sp. PCC 7001 (bacteria) / Gene: rbcL, cbbL, CPCC7001_1083 / Production host: Cyanobium sp. PCC 7001 (bacteria) References: UniProt: A5CKD0, ribulose-bisphosphate carboxylase #2: Protein | Mass: 12967.611 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Cyanobium sp. PCC 7001 (bacteria) / Gene: CPCC7001_1801 / Production host: Cyanobium sp. PCC 7001 (bacteria) / References: UniProt: B5ILN2 |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: subtomogram averaging |
-Sample preparation
Component | Name: Structure of Rubisco within Cyanobium carboxysome / Type: COMPLEX / Entity ID: all / Source: NATURAL |
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Source (natural) | Organism: Cyanobium sp. PCC 7001 (bacteria) |
Buffer solution | pH: 8 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-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: 5000 nm / Nominal defocus min: 2500 nm |
Image recording | Electron dose: 3.65 e/Å2 / Avg electron dose per subtomogram: 150 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
Software | Name: PHENIX / Version: 1.20_4459: / Classification: refinement | ||||||||||||||||||||||||
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EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
Symmetry | Point symmetry: D4 (2x4 fold dihedral) | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 152317 / Algorithm: FOURIER SPACE / Symmetry type: POINT | ||||||||||||||||||||||||
EM volume selection | Num. of tomograms: 139 / Num. of volumes extracted: 152317 | ||||||||||||||||||||||||
Atomic model building | Protocol: AB INITIO MODEL / Space: REAL | ||||||||||||||||||||||||
Refine LS restraints |
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