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Yorodumi- PDB-4v5y: Crystal structure of the bacterial ribosome from Escherichia coli... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 4v5y | |||||||||
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| Title | Crystal structure of the bacterial ribosome from Escherichia coli in complex with paromomycin and ribosome recycling factor (RRF). | |||||||||
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Keywords | RIBOSOME / RNA-protein complex | |||||||||
| Function / homology | Function and homology informationstringent response / ribosomal large subunit binding / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity / positive regulation of ribosome biogenesis ...stringent response / ribosomal large subunit binding / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity / positive regulation of ribosome biogenesis / RNA-binding transcription regulator activity / translational termination / negative regulation of cytoplasmic translation / four-way junction DNA binding / DnaA-L2 complex / translation repressor activity / negative regulation of translational initiation / regulation of mRNA stability / negative regulation of DNA-templated DNA replication initiation / mRNA regulatory element binding translation repressor activity / assembly of large subunit precursor of preribosome / positive regulation of RNA splicing / cytosolic ribosome assembly / regulation of DNA-templated transcription elongation / response to reactive oxygen species / ribosome assembly / transcription elongation factor complex / DNA endonuclease activity / transcription antitermination / regulation of cell growth / DNA-templated transcription termination / response to radiation / maintenance of translational fidelity / mRNA 5'-UTR binding / regulation of translation / large ribosomal subunit / ribosome biogenesis / ribosome binding / 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 / response to antibiotic / negative regulation of DNA-templated transcription / mRNA binding / DNA binding / RNA binding / zinc ion binding / membrane / cytoplasm / cytosol Similarity search - Function | |||||||||
| Biological species | ![]() ![]() Thermus thermophilus (bacteria) | |||||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.45 Å | |||||||||
Authors | Borovinskaya, M.A. / Pai, R.D. / Zhang, W. / Schuwirth, B.-S. / Holton, J.M. / Hirokawa, G. / Kaji, H. / Kaji, A. / Cate, J.H.D. | |||||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2007Title: Structural basis for aminoglycoside inhibition of bacterial ribosome recycling. Authors: Borovinskaya, M.A. / Pai, R.D. / Zhang, W. / Schuwirth, B.S. / Holton, J.M. / Hirokawa, G. / Kaji, H. / Kaji, A. / Cate, J.H. | |||||||||
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| Remark 999 | SEQUENCE Residue N ALA 35 and Residue N ARG 40 are linked together. |
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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 | 4v5y.cif.gz | 6.4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb4v5y.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 4v5y.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 4v5y_validation.pdf.gz | 2.6 MB | Display | wwPDB validaton report |
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| Full document | 4v5y_full_validation.pdf.gz | 4.3 MB | Display | |
| Data in XML | 4v5y_validation.xml.gz | 844.5 KB | Display | |
| Data in CIF | 4v5y_validation.cif.gz | 1.2 MB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v5/4v5y ftp://data.pdbj.org/pub/pdb/validation_reports/v5/4v5y | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 4v52C ![]() 4v53C ![]() 4v54C ![]() 4v55C ![]() 2avy ![]() 2aw4 ![]() 2aw7 ![]() 2awb S: Starting model for refinement 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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| 1 | ![]()
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| 2 | ![]()
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| Unit cell |
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Components
-RNA chain , 3 types, 6 molecules AACABADABBDB
| #1: RNA chain | Mass: 499690.031 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #22: RNA chain | Mass: 38790.090 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #23: RNA chain | Mass: 941612.375 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-30S ribosomal protein ... , 20 types, 40 molecules ACCCADCDAECEAFCFAGCGAHCHAICIAJCJAKCKALCLAMCMANCNAOCOAPCPAQCQ...
| #2: Protein | Mass: 25900.117 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Protein | Mass: 23383.002 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | Mass: 17498.203 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | Mass: 15727.512 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | Mass: 19923.959 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #7: Protein | Mass: 14015.361 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #8: Protein | Mass: 14755.074 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein | Mass: 11755.597 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #10: Protein | Mass: 13739.778 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #11: Protein | Mass: 13636.961 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein | Mass: 12997.271 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #13: Protein | Mass: 11475.364 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #14: Protein | Mass: 10290.816 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #15: Protein | Mass: 9207.572 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #16: Protein | Mass: 9593.296 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #17: Protein | Mass: 8874.276 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #18: Protein | Mass: 10324.160 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #19: Protein | Mass: 9577.268 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #20: Protein | Mass: 26650.475 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #21: Protein | Mass: 8392.844 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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+50S ribosomal protein ... , 30 types, 60 molecules BIDIBCDCBDDDBKDKBPDPBEDEBYDYB0D0B4D4B1D1B3D3BVDVB2D2BLDLBMDM...
-Non-polymers , 4 types, 1976 molecules 






| #54: Chemical | ChemComp-MG / #55: Chemical | ChemComp-PAR / #56: Chemical | #57: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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Sample preparation
| Crystal | Density Matthews: 3.37 Å3/Da / Density % sol: 63.53 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Crystal grow | Temperature: 277 K / Method: batch / pH: 7.5 Details: MPD, PEG 8000, MgCl2, NH4Cl, spermine, spermidine, TRIS, EDTA, pH 7.5, batch, temperature 277K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Components of the solutions |
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-Data collection
| Diffraction | Mean temperature: 93 K |
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| Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 12.3.1 / Wavelength: 1.111 Å |
| Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Mar 2, 2007 |
| Radiation | Monochromator: Double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1.111 Å / Relative weight: 1 |
| Reflection | Resolution: 4.45→69 Å / Num. obs: 341454 / % possible obs: 95.6 % / Redundancy: 3.5 % / Rmerge(I) obs: 0.096 / Net I/σ(I): 11.7 |
| Reflection shell | Resolution: 4.45→4.53 Å / Redundancy: 2.4 % / Rmerge(I) obs: 0.499 / Mean I/σ(I) obs: 2 / % possible all: 91.9 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 2AVY,2AW4,2AW7,2AWB Resolution: 4.45→40 Å / Isotropic thermal model: grouped by residue / σ(F): 0 / Stereochemistry target values: Torsional dynamics
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| Refinement step | Cycle: LAST / Resolution: 4.45→40 Å
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| Refine LS restraints |
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About Yorodumi




Thermus thermophilus (bacteria)
X-RAY DIFFRACTION
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