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Yorodumi- PDB-4v8o: Crystal structure of the hybrid state of ribosome in complex with... -
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-Basic information
Entry | Database: PDB / ID: 4v8o | |||||||||
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Title | Crystal structure of the hybrid state of ribosome in complex with the guanosine triphosphatase release factor 3 | |||||||||
Components |
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Keywords | RIBOSOME / HYBRID STATE / P/E TRNA / GUANOSINE TRIPHOSPHATASE / RELEASE FACTOR 3 | |||||||||
Function / homology | Function and homology information regulation of translational termination / translation release factor activity, codon specific / guanosine tetraphosphate binding / large ribosomal subunit / regulation of translation / ribosomal small subunit assembly / large ribosomal subunit rRNA binding / 5S rRNA binding / transferase activity / small ribosomal subunit ...regulation of translational termination / translation release factor activity, codon specific / guanosine tetraphosphate binding / large ribosomal subunit / regulation of translation / ribosomal small subunit assembly / large ribosomal subunit rRNA binding / 5S rRNA binding / transferase activity / small ribosomal subunit / cytosolic small ribosomal subunit / ribosomal large subunit assembly / cytosolic large ribosomal subunit / tRNA binding / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / GTPase activity / mRNA binding / GTP binding / zinc ion binding / metal ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | THERMUS THERMOPHILUS (bacteria) ESCHERICHIA COLI (E. coli) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.8 Å | |||||||||
Authors | Jin, H. / Kelley, A.C. / Ramakrishnan, V. | |||||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2011 Title: Crystal Structure of the Hybrid State of Ribosome in Complex with the Guanosine Triphosphatase Release Factor 3. Authors: Jin, H. / Kelley, A.C. / Ramakrishnan, V. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4v8o.cif.gz | 3.6 MB | Display | PDBx/mmCIF format |
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PDB format | pdb4v8o.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 4v8o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4v8o_validation.pdf.gz | 1.3 MB | Display | wwPDB validaton report |
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Full document | 4v8o_full_validation.pdf.gz | 3.1 MB | Display | |
Data in XML | 4v8o_validation.xml.gz | 591.1 KB | Display | |
Data in CIF | 4v8o_validation.cif.gz | 812.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v8/4v8o ftp://data.pdbj.org/pub/pdb/validation_reports/v8/4v8o | HTTPS FTP |
-Related structure data
Related structure data | 2j00 2jl7 S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-RNA chain , 5 types, 5 molecules AAAVAXBABB
#1: RNA chain | Mass: 493958.281 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: CHAIN A (16S RNA) HAS E.COLI NUMBERING, BASED ON A STRUCTURAL ALIGNMENT WITH THE CORRESPONDING E. COLI STRUCTURE IN 2AVY. Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: GenBank: 55979969 |
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#22: RNA chain | Mass: 24802.785 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Strain: K-12 |
#23: RNA chain | Mass: 2887.814 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ESCHERICHIA COLI (E. coli) |
#35: RNA chain | Mass: 947975.500 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: CHAIN A (23S RNA) HAS E.COLI RESIDUE NUMBERING, BASED ON A STRUCTURAL ALIGNMENT WITH THE CORRESPONDING E. COLI STRUCTURE IN 2AW4 Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: GenBank: 55979969 |
#36: RNA chain | Mass: 39540.617 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: GenBank: 55979969 |
-30S RIBOSOMAL PROTEIN ... , 20 types, 20 molecules ABACADAEAFAGAHAIAJAKALAMANAOAPAQARASATAU
#2: Protein | Mass: 29317.703 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: UniProt: P80371 |
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#3: Protein | Mass: 26751.076 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: UniProt: P80372 |
#4: Protein | Mass: 24373.447 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: UniProt: P80373 |
#5: Protein | Mass: 17583.416 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: UniProt: Q5SHQ5 |
#6: Protein | Mass: 11988.753 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: UniProt: Q5SLP8 |
#7: Protein | Mass: 18050.973 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: UniProt: P17291 |
#8: Protein | Mass: 15868.570 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: UniProt: Q5SHQ2, UniProt: A0A0M9AFS9*PLUS |
#9: Protein | Mass: 14429.661 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: UniProt: P80374 |
#10: Protein | Mass: 11954.968 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: UniProt: Q5SHN7 |
#11: Protein | Mass: 13737.868 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: UniProt: P80376 |
#12: Protein | Mass: 14920.754 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: UniProt: Q5SHN3 |
#13: Protein | Mass: 14338.861 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: UniProt: P80377 |
#14: Protein | Mass: 7158.725 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: UniProt: Q5SHQ1, UniProt: A0A0N0BLP2*PLUS |
#15: Protein | Mass: 10578.407 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: UniProt: Q5SJ76 |
#16: Protein | Mass: 10409.983 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: UniProt: Q5SJH3 |
#17: Protein | Mass: 12325.655 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: UniProt: Q5SHP7, UniProt: A0A0N0BLS5*PLUS |
#18: Protein | Mass: 10258.299 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: UniProt: Q5SLQ0 |
#19: Protein | Mass: 10605.464 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: UniProt: Q5SHP2 |
#20: Protein | Mass: 11736.143 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: UniProt: P80380 |
#21: Protein/peptide | Mass: 3350.030 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Variant: MRC-MSAW1 / Strain: HB8 / References: UniProt: Q5SIH3 |
+50S RIBOSOMAL PROTEIN ... , 31 types, 31 molecules B0B1B2B3B4B5B6B7B8B9BCBDBEBFBGBHBJBKBNBOBPBQBRBSBTBUBVBWBXBYBZ
-Protein / Non-polymers , 2 types, 2 molecules AY
#24: Protein | Mass: 59651.934 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: DH10B / Strain: K-12 / References: UniProt: B1XFI4 |
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#58: Chemical | ChemComp-GCP / |
-Details
Has protein modification | Y |
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Sequence details | AUTHOR REQUESTED CHANGE IN RESIDUE NUMBERING FOR CHAIN V ON 23-SEP-2011 AFTER THE RELEASE DEADLINE. ...AUTHOR REQUESTED CHANGE IN RESIDUE NUMBERING FOR CHAIN V ON 23-SEP-2011 AFTER THE RELEASE DEADLINE. THIS CHANGE WAS MADE AS A PART OF A REVDAT ON 30-MAY-2012. |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 9 |
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-Sample preparation
Crystal | Density Matthews: 3.14 Å3/Da / Density % sol: 60.87 % / Description: NONE |
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Crystal grow | pH: 6.7 Details: 100 MM MES-KOH PH 6.7, 20 MM KCL, 7.4% (W/V) PEG20K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 |
Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: Mar 27, 2011 / Details: DYNAMICALLY BENDABLE MIRROR |
Radiation | Monochromator: LN2 COOLED FIXED-EXIT SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.8→45 Å / Num. obs: 274830 / % possible obs: 99 % / Observed criterion σ(I): 1.3 / Redundancy: 7.44 % / Biso Wilson estimate: 40.1 Å2 / Rmerge(I) obs: 0.18 / Net I/σ(I): 6.42 |
Reflection shell | Resolution: 3.8→3.9 Å / Redundancy: 7.29 % / Rmerge(I) obs: 1.4 / Mean I/σ(I) obs: 1.06 / % possible all: 99 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2J00 2j00 Resolution: 3.8→44.9 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 10000101 / Data cutoff low absF: 0 / Cross valid method: THROUGHOUT / σ(F): 0 Details: THERE IS A LIGAND GDPCP IN THE COORDINATE IN THIS ENTRY. DUE TO THE RELATIVE WEAKER DENSITY OF THE RELEASE FACTOR 3 COMPARED TO THE RIBOSOME, THE CONFORMATION OF THE SIDE CHAINS OF RF3, AND ...Details: THERE IS A LIGAND GDPCP IN THE COORDINATE IN THIS ENTRY. DUE TO THE RELATIVE WEAKER DENSITY OF THE RELEASE FACTOR 3 COMPARED TO THE RIBOSOME, THE CONFORMATION OF THE SIDE CHAINS OF RF3, AND OF THE PRECISE REGISTRY IN REGIONS THAT HAD MOVED RELATIVE TO THE ISOLATED CRYSTAL STRUCTURE (PDB CODE: 2H5E) CAN NOT BE CERTAIN. IONS SUCH AS MG2+ AND WATER MOLECULES WERE NOT FITTED INTO THE STRUCTURE.
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 7.66545 Å2 / ksol: 0.2 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 147 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 3.8→44.9 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.8→4.04 Å / Rfactor Rfree error: 0.014 / Total num. of bins used: 6
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