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Open data
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Basic information
| Entry | Database: PDB / ID: 4v9c | |||||||||
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| Title | Allosteric control of the ribosome by small-molecule antibiotics | |||||||||
Components |
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Keywords | Ribosome/Antibiotic / Nucleic Acid Conformation / Protein Biosynthesis / antibiotic / neomycin / aminoglycoside / RRF / recycling / Ribosome-Antibiotic complex | |||||||||
| Function / homology | Function and homology informationcytoplasmic translational termination / 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 ...cytoplasmic translational termination / 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 / 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 / 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 | ![]() | |||||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 3.3 Å | |||||||||
Authors | Cate, J.H.D. / Pulk, A. / Blanchard, S.C. / Wang, L. / Feldman, M.B. / Wasserman, M.R. / Altman, R. | |||||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2012Title: Allosteric control of the ribosome by small-molecule antibiotics. Authors: Wang, L. / Pulk, A. / Wasserman, M.R. / Feldman, M.B. / Altman, R.B. / Doudna Cate, J.H. / Blanchard, S.C. | |||||||||
| History |
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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 | 4v9c.cif.gz | 7.4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb4v9c.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 4v9c.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 4v9c_validation.pdf.gz | 6.4 MB | Display | wwPDB validaton report |
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| Full document | 4v9c_full_validation.pdf.gz | 8.7 MB | Display | |
| Data in XML | 4v9c_validation.xml.gz | 1 MB | Display | |
| Data in CIF | 4v9c_validation.cif.gz | 1.3 MB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v9/4v9c ftp://data.pdbj.org/pub/pdb/validation_reports/v9/4v9c | HTTPS FTP |
-Related structure data
| 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 , 5 types, 10 molecules AACAAVCVAXCXBADABBDB
| #1: RNA chain | Mass: 499690.031 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #22: RNA chain | Mass: 24485.539 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #23: RNA chain | Mass: 7787.751 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: RNA oligonucleotide #24: RNA chain | Mass: 941612.375 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #25: RNA chain | Mass: 38790.090 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 ABCBACCCADCDAECEAFCFAGCGAHCHAICIAJCJAKCKALCLAMCMANCNAOCOAPCP...
| #2: Protein | Mass: 26781.670 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Protein | Mass: 26031.316 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | Mass: 23514.199 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | Mass: 17629.398 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | Mass: 15727.512 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #7: Protein | Mass: 20055.156 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #8: Protein | Mass: 14146.557 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein | Mass: 14886.270 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #10: Protein | Mass: 11755.597 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #11: Protein | Mass: 13870.975 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein | Mass: 13768.157 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #13: Protein | Mass: 13128.467 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #14: Protein | Mass: 11606.560 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #15: Protein | Mass: 10290.816 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #16: Protein | Mass: 9207.572 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #17: Protein | Mass: 9724.491 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #18: Protein | Mass: 9005.472 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #19: Protein | Mass: 10455.355 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #20: Protein | Mass: 9708.464 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #21: Protein | Mass: 8524.039 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 BCDCBDDDBEDEBFDFBGDGBHDHBIDIBJDJBKDKBLDLBMDMBNDNBODOBPDPBQDQ...
-Protein , 1 types, 1 molecules CY
| #55: Protein | Mass: 20671.621 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 4 types, 2237 molecules 






| #56: Chemical | ChemComp-MG / #57: Chemical | ChemComp-NMY / #58: Chemical | #59: Water | ChemComp-HOH / | |
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-Details
| Has protein modification | Y |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 16 |
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Sample preparation
| Crystal | Density Matthews: 3.2 Å3/Da / Density % sol: 61.51 % |
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| Crystal grow | Temperature: 291 K / pH: 6.5 / Details: PEG800, MPD, pH 6.5, microbatch, temperature 291K |
-Data collection
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| Detector |
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| Radiation |
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| Radiation wavelength | Wavelength: 1.111 Å / Relative weight: 1 | |||||||||||||||
| Reflection | Highest resolution: 3.3 Å / Num. obs: 793808 / % possible obs: 95.2 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 98.37 Å2 / Rmerge(I) obs: 0.182 / Net I/σ(I): 5.76 | |||||||||||||||
| Reflection shell | Resolution: 3.3→3.39 Å / Rmerge(I) obs: 0.868 / Mean I/σ(I) obs: 1.12 / % possible all: 86.1 |
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Processing
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| Refinement | Method to determine structure: FOURIER SYNTHESIS / Resolution: 3.3→70 Å / Occupancy max: 1 / Occupancy min: 0.59 / σ(F): 3.3 / Stereochemistry target values: ENGH & HUBER
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| Displacement parameters | Biso mean: 151.1 Å2 | ||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 3.3→70 Å
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X-RAY DIFFRACTION
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