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Open data
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Basic information
| Entry | Database: PDB / ID: 6spg | ||||||||||||||||||||||||||||||||||||
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| Title | Pseudomonas aeruginosa 70s ribosome from a clinical isolate | ||||||||||||||||||||||||||||||||||||
Components |
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Keywords | RIBOSOME / Pseudomonas aeruginosa | ||||||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationlarge ribosomal subunit / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / cytosolic small ribosomal subunit ...large ribosomal subunit / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / mRNA binding / RNA binding / metal ion binding / cytoplasm / cytosol Similarity search - Function | ||||||||||||||||||||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.34 Å | ||||||||||||||||||||||||||||||||||||
Authors | Halfon, Y. / Jimenez-Fernande, A. / La Ros, R. / Espinos, R. / Krogh Johansen, H. / Matzov, D. / Eyal, Z. / Bashan, A. / Zimmerman, E. / Belousoff, M. ...Halfon, Y. / Jimenez-Fernande, A. / La Ros, R. / Espinos, R. / Krogh Johansen, H. / Matzov, D. / Eyal, Z. / Bashan, A. / Zimmerman, E. / Belousoff, M. / Molin, S. / Yonath, A. | ||||||||||||||||||||||||||||||||||||
| Funding support | Denmark, 4items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2019Title: Structure of ribosomes from an aminoglycoside-resistant clinical isolate. Authors: Yehuda Halfon / Alicia Jimenez-Fernandez / Ruggero La Rosa / Rocio Espinosa Portero / Helle Krogh Johansen / Donna Matzov / Zohar Eyal / Anat Bashan / Ella Zimmerman / Matthew Belousoff / ...Authors: Yehuda Halfon / Alicia Jimenez-Fernandez / Ruggero La Rosa / Rocio Espinosa Portero / Helle Krogh Johansen / Donna Matzov / Zohar Eyal / Anat Bashan / Ella Zimmerman / Matthew Belousoff / Søren Molin / Ada Yonath / ![]() Abstract: Resistance to antibiotics has become a major threat to modern medicine. The ribosome plays a fundamental role in cell vitality by the translation of the genetic code into proteins; hence, it is a ...Resistance to antibiotics has become a major threat to modern medicine. The ribosome plays a fundamental role in cell vitality by the translation of the genetic code into proteins; hence, it is a major target for clinically useful antibiotics. We report here the cryo-electron microscopy structures of the ribosome of a pathogenic aminoglycoside (AG)-resistant strain, as well as of a nonresistance strain isolated from a cystic fibrosis patient. The structural studies disclosed defective ribosome complex formation due to a conformational change of rRNA helix H69, an essential intersubunit bridge, and a secondary binding site of the AGs. In addition, a stable conformation of nucleotides A1486 and A1487, pointing into helix h44, is created compared to a non-AG-bound ribosome. We suggest that altering the conformations of ribosomal protein uL6 and rRNA helix H69, which interact with initiation-factor IF2, interferes with proper protein synthesis initiation. | ||||||||||||||||||||||||||||||||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 6spg.cif.gz | 3.1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb6spg.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 6spg.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 6spg_validation.pdf.gz | 1.3 MB | Display | wwPDB validaton report |
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| Full document | 6spg_full_validation.pdf.gz | 1.4 MB | Display | |
| Data in XML | 6spg_validation.xml.gz | 207.1 KB | Display | |
| Data in CIF | 6spg_validation.cif.gz | 359.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sp/6spg ftp://data.pdbj.org/pub/pdb/validation_reports/sp/6spg | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 10285MC ![]() 6spbC ![]() 6spcC ![]() 6spdC ![]() 6speC ![]() 6spfC M: map data used to model this data C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-RNA chain , 3 types, 3 molecules aAB
| #1: RNA chain | Mass: 494643.906 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #22: RNA chain | Mass: 935990.438 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #23: RNA chain | Mass: 37679.391 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-30S ribosomal protein ... , 20 types, 20 molecules bcdefghijklmnopqrstu
| #2: Protein | Mass: 26684.766 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #3: Protein | Mass: 23438.215 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #4: Protein | Mass: 23187.473 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #5: Protein | Mass: 16432.092 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #6: Protein | Mass: 12278.832 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #7: Protein | Mass: 17313.199 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #8: Protein | Mass: 14059.415 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #9: Protein | Mass: 14139.195 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein | Mass: 10886.569 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #11: Protein | Mass: 12086.657 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #12: Protein | Mass: 13569.727 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #13: Protein | Mass: 12307.191 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #14: Protein | Mass: 11203.024 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #15: Protein | Mass: 9776.193 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #16: Protein | Mass: 8762.938 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #17: Protein | Mass: 8848.358 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #18: Protein | Mass: 8346.693 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #19: Protein | Mass: 9182.882 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #20: Protein | Mass: 9426.062 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #21: Protein | Mass: 7519.769 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+50S ribosomal protein ... , 29 types, 29 molecules CDEFGHIJKLMNOPQRSTUVWXZ123456
-Protein / Non-polymers , 2 types, 173 molecules Y

| #46: Protein | Mass: 6807.757 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #54: Chemical | ChemComp-MG / |
-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: Pseudomonas aeruginosa 70s ribosome from a clinical isolate Type: RIBOSOME / Entity ID: #1-#53 / 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 |
| Specimen support | Grid material: COPPER / Grid mesh size: 200 divisions/in. / Grid type: Quantifoil R2/2 |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K |
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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 |
| Image recording | Electron dose: 1 e/Å2 / Film or detector model: FEI FALCON II (4k x 4k) |
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Processing
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| CTF correction | Type: NONE | ||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||
| 3D reconstruction | Resolution: 3.34 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 128795 / Symmetry type: POINT |
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Denmark, 4items
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