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Yorodumi- PDB-4v53: 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: 4v53 | |||||||||
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| Title | Crystal structure of the bacterial ribosome from Escherichia coli in complex with gentamicin. | |||||||||
 Components | 
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 Keywords | RIBOSOME / RNA-protein complex | |||||||||
| Function / homology |  Function and homology informationstringent response / 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 ...stringent response / 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 / ribosome assembly / regulation of DNA-templated transcription elongation / transcription elongation factor complex / cytosolic ribosome assembly / response to reactive oxygen species / DNA endonuclease activity / transcription antitermination / regulation of cell growth / DNA-templated transcription termination / response to radiation / maintenance of translational fidelity / mRNA 5'-UTR binding / ribosome biogenesis / large ribosomal subunit / regulation of translation / ribosome binding / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / small ribosomal subunit rRNA binding / ribosomal large subunit assembly / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / 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 | ![]()  | |||||||||
| Method |  X-RAY DIFFRACTION /  SYNCHROTRON /  MOLECULAR REPLACEMENT / Resolution: 3.54 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.  | |||||||||
| History | 
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| Remark 300 | BIOMOLECULE: 1, 2 THIS ENTRY CONTAINS PART OF THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT. THE BIOLOGICAL ...BIOMOLECULE: 1, 2 THIS ENTRY CONTAINS PART OF THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT. THE BIOLOGICAL UNIT CONSISTS OF TWO SUBUNITS. THERE ARE 2 BIOLOGICAL UNITS IN THE ASYMMETRIC UNIT. | 
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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 |  4v53.cif.gz | 6.3 MB | Display |  PDBx/mmCIF format | 
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| PDB format |  pdb4v53.ent.gz | Display |  PDB format | |
| PDBx/mmJSON format |  4v53.json.gz | Tree view |  PDBx/mmJSON format | |
| Others |  Other downloads | 
-Validation report
| Summary document |  4v53_validation.pdf.gz | 3.8 MB | Display |  wwPDB validaton report | 
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| Full document |  4v53_full_validation.pdf.gz | 5.5 MB | Display | |
| Data in XML |  4v53_validation.xml.gz | 818 KB | Display | |
| Data in CIF |  4v53_validation.cif.gz | 1.1 MB | Display | |
| Arichive directory |  https://data.pdbj.org/pub/pdb/validation_reports/v5/4v53 ftp://data.pdbj.org/pub/pdb/validation_reports/v5/4v53 | HTTPS FTP  | 
-Related structure data
| Related structure data | ![]() 4v52C ![]() 4v54C ![]() 4v55C ![]() 4v5yC ![]() 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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| Details | The biological unit consists of two subunits. There are 2 biological units in the asymmetric unit | 
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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  ... , 29 types, 58 molecules BIDIBCDCBDDDBKDKBPDPBEDEBYDYB0D0B4D4B1D1B3D3BVDVB2D2BLDLBMDM...                              
-Non-polymers , 4 types, 1980 molecules 






| #53: Chemical | ChemComp-MG / #54: Chemical | ChemComp-LLL / ( #55: Chemical | #56: Water |  ChemComp-HOH /  |  | 
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-Experimental details
-Experiment
| Experiment | Method:  X-RAY DIFFRACTION / Number of used crystals: 19  | 
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Sample preparation
| Crystal | Density Matthews: 3.41 Å3/Da / Density % sol: 63.98 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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 5, 2006 | 
| 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: 3.54→139 Å / Num. obs: 627888 / % possible obs: 90.2 % / Redundancy: 4.8 % / Rmerge(I) obs: 0.102 / Net I/σ(I): 10.6 | 
| Reflection shell | Resolution: 3.54→3.81 Å / Redundancy: 1.6 % / Rmerge(I) obs: 0.47 / Mean I/σ(I) obs: 2 / % possible all: 54.8 | 
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Processing
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| Refinement | Method to determine structure:  MOLECULAR REPLACEMENTStarting model: 2AVY, 2AW4, 2AW7, 2AWB Resolution: 3.54→70 Å / Isotropic thermal model: grouped by residue / σ(F): 0 / Stereochemistry target values: torsional dynamics 
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| Displacement parameters | Biso mean: 84.396 Å2 | ||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 3.54→70 Å
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| Refine LS restraints | 
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