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Open data
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Basic information
| Entry | Database: PDB / ID: 9p38 | ||||||
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| Title | YsxC-GMPPNP treated 44.5SYsxC particles. Class 1. | ||||||
Components |
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Keywords | RIBOSOME / 44.5S particle / YsxC | ||||||
| Function / homology | Function and homology informationdivision septum assembly / large ribosomal subunit / ribosomal large subunit assembly / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation ...division septum assembly / large ribosomal subunit / ribosomal large subunit assembly / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / mRNA binding / GTP binding / metal ion binding / cytoplasm / cytosol Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.5 Å | ||||||
Authors | Ortega, J. / Seffouh, A. | ||||||
| Funding support | Canada, 1items
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Citation | Journal: Nucleic Acids Res / Year: 2025Title: YsxC is a placeholder for ribosomal protein uL2 during 50S ribosomal subunit assembly. Authors: Amal Seffouh / Dominic Arpin / Kaustuv Basu / Joaquin Ortega / ![]() Abstract: The maturation of the functional core of the 50S ribosomal subunit in Bacillus subtilis is assisted by assembly factors that enhance the efficiency of the process. Two essential assembly factors, the ...The maturation of the functional core of the 50S ribosomal subunit in Bacillus subtilis is assisted by assembly factors that enhance the efficiency of the process. Two essential assembly factors, the GTPases RbgA and YphC, bind at or near the functional sites of the 50S subunit to promote the folding of ribosomal RNA helices that play key functional roles. YsxC is another GTPase involved in the maturation of the 50S subunit, whose function remains unknown. We demonstrate that YsxC aids 50S assembly through a drastically different mechanism. YsxC binds in the body of the 44.5S large ribosome assembly intermediate, occupying the site where uL2 binds and controls the timing in the folding of rRNA helices forming the binding site for uL2. It creates a "primordial" binding site that includes six out of the eleven rRNA helices forming the uL2 mature binding site. Once YsxC is released, uL2 binds to this "primordial" binding site, and the remaining helices that stabilize uL2 fold, and the entire region adopts the mature conformation. This role of YsxC functioning as a placeholder factor for ribosomal protein uL2 provides the first example of such a factor's involvement in the ribosome assembly process in bacteria. | ||||||
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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 | 9p38.cif.gz | 1.5 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9p38.ent.gz | 1.2 MB | Display | PDB format |
| PDBx/mmJSON format | 9p38.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9p38_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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| Full document | 9p38_full_validation.pdf.gz | 1.6 MB | Display | |
| Data in XML | 9p38_validation.xml.gz | 104.8 KB | Display | |
| Data in CIF | 9p38_validation.cif.gz | 178.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p3/9p38 ftp://data.pdbj.org/pub/pdb/validation_reports/p3/9p38 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 71238MC ![]() 9p4iC 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
-50S ribosomal protein ... , 16 types, 16 molecules DEJKLNPQRSTUZbYd
| #2: Protein | Mass: 22723.348 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: rplC, B4122_1436, B4417_1506, ETA10_00730, ETK61_00730, ETK71_00730, SC09_Contig26orf00060 Production host: ![]() |
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| #3: Protein | Mass: 22424.951 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: rplD, B4122_1435, B4417_1507, ETK71_00735, SC09_Contig26orf00061 Production host: ![]() |
| #4: Protein | Mass: 16407.104 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: rplM, B4122_1403, B4417_1539, D3797_020925, ETA10_00900, ETK61_00900, ETK71_00900 Production host: ![]() |
| #5: Protein | Mass: 13175.288 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: rplN, B4122_1427, B4417_1515, CJ481_04140, D3797_021045, ETA10_00780, ETK61_00780, ETK71_00780, SC09_Contig26orf00070 Production host: ![]() |
| #6: Protein | Mass: 15410.694 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: rplO, B4122_1418, B4417_1524, D3797_021000, ETA10_00825, ETK61_00825, ETK71_00825 Production host: ![]() |
| #7: Protein | Mass: 13774.806 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: rplQ, B4122_1408, B4417_1534, CJ481_04045, D3797_020950, ETA10_00875, ETK61_00875, ETK71_00875, SC09_Contig26orf00091 Production host: ![]() |
| #8: Protein | Mass: 13416.853 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: rplS, B4122_2715, B4417_3551, CJ481_18820, D3797_012615, ETA10_08770, ETK61_09045, ETK71_08680, SC09_Contig19orf01139 Production host: ![]() |
| #9: Protein | Mass: 13537.993 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: rplT, B4122_3557, B4122_3823, B4417_0515, CJ481_11505, D3797_006720, ETA10_14785, ETK61_15815, ETK71_14810, SC09_Contig17orf00528 Production host: ![]() |
| #10: Protein | Mass: 11296.081 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: rplU, B4122_3686, B4417_0614, D3797_007210, ETA10_14315, ETK61_15045, ETK71_14340, SC09_Contig17orf00255 Production host: ![]() |
| #11: Protein | Mass: 12481.608 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: rplV, B4122_1432, B4417_1510, CJ481_04165, D3797_021070, ETA10_00755, ETK61_00755, ETK71_00755, KS08_00695, SC09_Contig26orf00065 Production host: ![]() |
| #12: Protein | Mass: 10978.813 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: rplW, B4122_1434, B4417_1508, ETA10_00740, ETK61_00740, ETK71_00740, KS08_00680, SC09_Contig26orf00062 Production host: ![]() |
| #13: Protein | Mass: 11166.120 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: rplX, B4122_1426, B4417_1516, CJ481_04135, D3797_021040, ETA10_00785, ETK61_00785, ETK71_00785, SC09_Contig26orf00072 Production host: ![]() |
| #14: Protein | Mass: 6650.795 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: rpmD, B4122_1419, B4417_1523, CJ481_04100, D3797_021005, ETA10_00820, ETK61_00820, ETK71_00820, KS08_00760, SC09_Contig26orf00079 Production host: ![]() |
| #15: Protein | Mass: 6745.073 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: rpmF, CJ481_19300, D3797_013100, ETA10_08290, ETK61_08565, ETK71_08200, KS08_07655 Production host: ![]() |
| #16: Protein | Mass: 7728.029 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: rpmC, B4122_1429, B4417_1513, CJ481_04150, D3797_021055, ETA10_00770, ETK61_00770, ETK71_00770, KS08_00710, SC09_Contig26orf00068 Production host: ![]() |
| #17: Protein/peptide | Mass: 5271.332 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: rpmH, CJ481_04925, D3797_000040, ETA10_21790, ETK61_22795, ETK71_21425, KS08_20020 Production host: ![]() |
-RNA chain / Protein , 2 types, 2 molecules AB
| #18: Protein | Mass: 22060.414 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: yihA, engB, B4122_3751, J5227_02435, P5633_09985, SC09_Contig17orf00345 Production host: ![]() |
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| #1: RNA chain | Mass: 949300.062 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Details
| Has protein modification | Y |
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-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: YsxC-GMPPNP treated 44.5SYsxC particles. Class 1. / Type: RIBOSOME / Entity ID: all / Source: NATURAL |
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| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.4 |
| 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: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 1000 nm |
| Image recording | Electron dose: 40 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 | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 873768 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 2.5 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi






Canada, 1items
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FIELD EMISSION GUN