[English] 日本語
Yorodumi- PDB-4v9d: Structures of the bacterial ribosome in classical and hybrid stat... -
+
Open data
-
Basic information
| Entry | Database: PDB / ID: 4v9d | |||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Title | Structures of the bacterial ribosome in classical and hybrid states of tRNA binding | |||||||||
Components |
| |||||||||
Keywords | RIBOSOME / Protein biosynthesis / RNA / tRNA / transfer RNA / 30S / 70S / 16S / ribosomal subunit / ribosome recycling factor / RRF | |||||||||
| 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 Å | |||||||||
Authors | Dunkle, J.A. / Wang, L. / Feldman, M.B. / Pulk, A. / Chen, V.B. / Kapral, G.J. / Noeske, J. / Richardson, J.S. / Blanchard, S.C. / Cate, J.H.D. | |||||||||
Citation | Journal: Science / Year: 2011Title: Structures of the bacterial ribosome in classical and hybrid states of tRNA binding. Authors: Dunkle, J.A. / Wang, L. / Feldman, M.B. / Pulk, A. / Chen, V.B. / Kapral, G.J. / Noeske, J. / Richardson, J.S. / Blanchard, S.C. / Cate, J.H. | |||||||||
| History |
|
-
Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
|---|
-
Downloads & links
-
Download
| PDBx/mmCIF format | 4v9d.cif.gz | 6.6 MB | Display | PDBx/mmCIF format |
|---|---|---|---|---|
| PDB format | pdb4v9d.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 4v9d.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 4v9d_validation.pdf.gz | 1.6 MB | Display | wwPDB validaton report |
|---|---|---|---|---|
| Full document | 4v9d_full_validation.pdf.gz | 4.1 MB | Display | |
| Data in XML | 4v9d_validation.xml.gz | 927.3 KB | Display | |
| Data in CIF | 4v9d_validation.cif.gz | 1.3 MB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v9/4v9d ftp://data.pdbj.org/pub/pdb/validation_reports/v9/4v9d | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 3i1m ![]() 3i1n ![]() 3i1o ![]() 3i1p S: Starting model for refinement |
|---|---|
| Similar structure data |
-
Links
-
Assembly
| Deposited unit | ![]()
| ||||||||
|---|---|---|---|---|---|---|---|---|---|
| 1 | ![]()
| ||||||||
| 2 | ![]()
| ||||||||
| Unit cell |
|
-
Components
-RNA chain , 6 types, 10 molecules AABAAVBVAXBXCADACBDB
| #1: RNA chain | Mass: 498725.406 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 genetically manipulated source Source: (gene. exp.) ![]() ![]() #23: RNA chain | Mass: 5170.151 Da / Num. of mol.: 2 / Source method: obtained synthetically #25: RNA chain | Mass: 941306.188 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #26: RNA chain | | Mass: 38483.926 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #56: RNA chain | | Mass: 38177.762 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
|---|
-30S ribosomal protein ... , 20 types, 40 molecules ABBBACBCADBDAEBEAFBFAGBGAHBHAIBIAJBJAKBKALBLAMBMANBNAOBOAPBP...
| #2: Protein | Mass: 24253.943 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Protein | Mass: 23078.785 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | Mass: 23383.002 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | Mass: 15804.282 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | Mass: 11669.371 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #7: Protein | Mass: 16861.523 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #8: Protein | Mass: 14015.361 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein | Mass: 14554.882 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #10: Protein | Mass: 11196.988 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #11: Protein | Mass: 12487.200 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein | Mass: 13636.961 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #13: Protein | Mass: 12625.753 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #14: Protein | Mass: 11475.364 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #15: Protein | Mass: 10159.621 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: 9263.946 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #18: Protein | Mass: 6466.477 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #19: Protein | Mass: 9057.626 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #20: Protein | Mass: 9506.190 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #21: Protein | Mass: 6067.081 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
|---|
-Protein , 1 types, 1 molecules AY
| #24: Protein | Mass: 20322.174 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
|---|
+50S ribosomal protein ... , 30 types, 58 molecules CCDCCDDDCEDECFDFCGDGCHDHCIDICJDJCKDKCLDLCMDMCNDNCODOCPDPCQDQ...
-Non-polymers , 3 types, 2227 molecules 




| #58: Chemical | ChemComp-MG / #59: Chemical | #60: Water | ChemComp-HOH / | |
|---|
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 5 |
|---|
-
Sample preparation
| Crystal |
| ||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Crystal grow |
|
-Data collection
| Diffraction |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Diffraction source |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Detector |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation wavelength |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection | Resolution: 3→40 Å / Num. obs: 938380 / % possible obs: 83.5 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 51.273 Å2 / Rmerge(I) obs: 0.194 / Net I/σ(I): 7.38 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection shell | Diffraction-ID: 1,2,3
|
-
Processing
| Software |
| ||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Refinement | Method to determine structure: FOURIER SYNTHESISStarting model: PDB ENTRIES 3I1M, 3I1N, 3I1O, 3I1P Resolution: 3→40 Å / Occupancy max: 1 / Occupancy min: 1 / σ(F): 1.8 / Stereochemistry target values: PHENIX
| ||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso max: 170.12 Å2 / Biso mean: 41.6019 Å2 / Biso min: 0.01 Å2 | ||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 3→40 Å
|
Movie
Controller
About Yorodumi




X-RAY DIFFRACTION
Citation










PDBj

































