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Yorodumi- EMDB-39598: cryo-EM structure of carboxysomal midi-shell: icosahedral assembl... -
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Basic information
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| Title | cryo-EM structure of carboxysomal midi-shell: icosahedral assembly from CsoS4A/4B/1A/1B/1C/1D and CsoS2 C-terminal co-expression (T = 9) | |||||||||
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Keywords | Carboxysome / shell / Icosahedron / STRUCTURAL PROTEIN | |||||||||
| Function / homology | Function and homology informationstructural constituent of carboxysome shell / carboxysome / carbon fixation / viral translational frameshifting Similarity search - Function | |||||||||
| Biological species | Halothiobacillus neapolitanus (bacteria) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.3 Å | |||||||||
Authors | Wang P / Li JX / Li TP / Li K / Ng PC / Wang SM / Chriscoli V / Basle A / Marles-Wright J / Zhang YZ / Liu LN | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Sci Adv / Year: 2024Title: Molecular principles of the assembly and construction of a carboxysome shell. Authors: Peng Wang / Jianxun Li / Tianpei Li / Kang Li / Pei Cing Ng / Saimeng Wang / Vincent Chriscoli / Arnaud Basle / Jon Marles-Wright / Yu-Zhong Zhang / Lu-Ning Liu / ![]() Abstract: Intracellular compartmentalization enhances biological reactions, crucial for cellular function and survival. An example is the carboxysome, a bacterial microcompartment for CO fixation. The ...Intracellular compartmentalization enhances biological reactions, crucial for cellular function and survival. An example is the carboxysome, a bacterial microcompartment for CO fixation. The carboxysome uses a polyhedral protein shell made of hexamers, pentamers, and trimers to encapsulate Rubisco, increasing CO levels near Rubisco to enhance carboxylation. Despite their role in the global carbon cycle, the molecular mechanisms behind carboxysome shell assembly remain unclear. Here, we present a structural characterization of α-carboxysome shells generated from recombinant systems, which contain all shell proteins and the scaffolding protein CsoS2. Atomic-resolution cryo-electron microscopy of the shell assemblies, with a maximal size of 54 nm, unveil diverse assembly interfaces between shell proteins, detailed interactions of CsoS2 with shell proteins to drive shell assembly, and the formation of heterohexamers and heteropentamers by different shell protein paralogs, facilitating the assembly of larger empty shells. Our findings provide mechanistic insights into the construction principles of α-carboxysome shells and the role of CsoS2 in governing α-carboxysome assembly and functionality. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_39598.map.gz | 450.6 MB | EMDB map data format | |
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| Header (meta data) | emd-39598-v30.xml emd-39598.xml | 16.4 KB 16.4 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_39598_fsc.xml | 16.3 KB | Display | FSC data file |
| Images | emd_39598.png | 210 KB | ||
| Filedesc metadata | emd-39598.cif.gz | 5.5 KB | ||
| Others | emd_39598_half_map_1.map.gz emd_39598_half_map_2.map.gz | 442.5 MB 442.5 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-39598 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-39598 | HTTPS FTP |
-Validation report
| Summary document | emd_39598_validation.pdf.gz | 1.1 MB | Display | EMDB validaton report |
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| Full document | emd_39598_full_validation.pdf.gz | 1.1 MB | Display | |
| Data in XML | emd_39598_validation.xml.gz | 25.3 KB | Display | |
| Data in CIF | emd_39598_validation.cif.gz | 33.2 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-39598 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-39598 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8yveMC ![]() 8yvcC ![]() 8yvdC ![]() 8yvfC ![]() 8yviC ![]() 8yxuC ![]() 9f0hC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_39598.map.gz / Format: CCP4 / Size: 476.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.06 Å | ||||||||||||||||||||||||||||||||||||
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_39598_half_map_1.map | ||||||||||||
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-Half map: #2
| File | emd_39598_half_map_2.map | ||||||||||||
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Sample components
-Entire : Carboxysomal midi-shell:icosahedral assembly from CsoS4A/4B/1A/1B...
| Entire | Name: Carboxysomal midi-shell:icosahedral assembly from CsoS4A/4B/1A/1B/1C/1D and CsoS2 C-terminal co-expression (T = 9) |
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| Components |
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-Supramolecule #1: Carboxysomal midi-shell:icosahedral assembly from CsoS4A/4B/1A/1B...
| Supramolecule | Name: Carboxysomal midi-shell:icosahedral assembly from CsoS4A/4B/1A/1B/1C/1D and CsoS2 C-terminal co-expression (T = 9) type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: Halothiobacillus neapolitanus (bacteria) |
-Macromolecule #1: Major carboxysome shell protein CsoS1A
| Macromolecule | Name: Major carboxysome shell protein CsoS1A / type: protein_or_peptide / ID: 1 / Number of copies: 8 / Enantiomer: LEVO |
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| Source (natural) | Organism: Halothiobacillus neapolitanus (bacteria) |
| Molecular weight | Theoretical: 9.973478 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MADVTGIALG MIETRGLVPA IEAADAMTKA AEVRLVGRQF VGGGYVTVLV RGETGAVNAA VRAGADACER VGDGLVAAHI IARVHSEVE NILPKAPQA UniProtKB: Major carboxysome shell protein CsoS1A |
-Macromolecule #2: Carboxysome assembly protein CsoS2B
| Macromolecule | Name: Carboxysome assembly protein CsoS2B / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Halothiobacillus neapolitanus (bacteria) |
| Molecular weight | Theoretical: 29.358428 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MPFCTSTPEP EAQSTEQSLT CEGQIISGTS VDASDLVTGN EIGEQQLISG DAYVGAQQTG CLPTSPRFNQ TGNVQSMGFK NTNQPEQNF APGEVMPTDF SIQTPARSAQ NRITGNDIAP SGRITGPGML ATGLITGTPE FRHAARELVG SPQPMAMAMA N RNKAAQAP ...String: MPFCTSTPEP EAQSTEQSLT CEGQIISGTS VDASDLVTGN EIGEQQLISG DAYVGAQQTG CLPTSPRFNQ TGNVQSMGFK NTNQPEQNF APGEVMPTDF SIQTPARSAQ NRITGNDIAP SGRITGPGML ATGLITGTPE FRHAARELVG SPQPMAMAMA N RNKAAQAP VVQPEVVATQ EKPELVCAPR SDQMDRVSGE GKERCHITGD DWSVNKHITG TAGQWASGRN PSMRGNARVV ET SAFANRN VPKPEKPGSK ITGSSGNDTQ GSLITYSGGA RG UniProtKB: Carboxysome assembly protein CsoS2B |
-Macromolecule #3: Carboxysome shell vertex protein CsoS4A
| Macromolecule | Name: Carboxysome shell vertex protein CsoS4A / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Halothiobacillus neapolitanus (bacteria) |
| Molecular weight | Theoretical: 8.900287 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MKIMQVEKTL VSTNRIADMG HKPLLVVWEK PGAPRQVAVD AIGCIPGDWV LCVGSSAARE AAGSKSYPSD LTIIGIIDQW NGE UniProtKB: Carboxysome shell vertex protein CsoS4A |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.2 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Halothiobacillus neapolitanus (bacteria)
Authors
China, 1 items
Citation














Z (Sec.)
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Processing
FIELD EMISSION GUN


