+Open data
-Basic information
Entry | Database: PDB / ID: 4v4p | |||||||||
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Title | Crystal structure of 70S ribosome with thrS operator and tRNAs. | |||||||||
Components |
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Keywords | RIBOSOME / mRNA / translational operator | |||||||||
Function / homology | Function and homology information large ribosomal subunit / regulation of translation / ribosomal small subunit assembly / small ribosomal subunit / transferase activity / cytosolic small ribosomal subunit / cytosolic large ribosomal subunit / tRNA binding / rRNA binding / ribosome ...large ribosomal subunit / regulation of translation / ribosomal small subunit assembly / small ribosomal subunit / transferase activity / cytosolic small ribosomal subunit / cytosolic large ribosomal subunit / tRNA binding / rRNA binding / ribosome / structural constituent of ribosome / ribonucleoprotein complex / translation / mRNA binding / zinc ion binding / metal ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Thermus thermophilus (bacteria) Thermus thermophilus HB8 (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 5.5 Å | |||||||||
Authors | Jenner, L. / Romby, P. / Rees, B. / Schulze-Briese, C. / Springer, M. / Ehresmann, C. / Ehresmann, B. / Moras, D. / Yusupova, G. / Yusupov, M. | |||||||||
Citation | Journal: Science / Year: 2005 Title: Translational operator of mRNA on the ribosome: how repressor proteins exclude ribosome binding. Authors: Jenner, L. / Romby, P. / Rees, B. / Schulze-Briese, C. / Springer, M. / Ehresmann, C. / Ehresmann, B. / Moras, D. / Yusupova, G. / Yusupov, M. | |||||||||
History |
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Remark 400 | COMPOUND PDB ENTRIES 1YL3 AND 1YL4 REPRESENT ONE CRYSTAL STRUCTURE OF THE THERMUS THERMOPHILUS 70S ...COMPOUND PDB ENTRIES 1YL3 AND 1YL4 REPRESENT ONE CRYSTAL STRUCTURE OF THE THERMUS THERMOPHILUS 70S RIBOSOME. THIS FILE, 1YL3, CONTAINS THE 50S SUBUNIT. THE 30S RIBOSOMAL SUBUNIT WITH MRNA AND TRNAS IS IN FILE 1YL4. | |||||||||
Remark 999 | SEQUENCE Initial C alpha coordinates of most proteins were those of PDB entry 1giy, which is the ...SEQUENCE Initial C alpha coordinates of most proteins were those of PDB entry 1giy, which is the same ribosome subunit from the same organism (Th. thermophilus). This was completed with proteins from 1nkw (same ribosome subunit from Deinococcus radiodurans), and structures of isolated proteins whenever available. The sequence of this subunit represent that of pdb entry 1giy. Proteins L20, L21, L25, L27, and L31 to L36 in the initial model were those of entry 1nkw and have the Deinococcus radiodurans sequence. The dbref is provided only for the sequences that match the relevant proteins from T. thermophilus. Residues (D ALA 216 ) and (D PRO 222 ) are linked together, Residues (E THR 49 ) and (E PRO 61 ) are linked together, Residues (E GLU 66 ) and (E THR 67 ) are linked together, Residues (E GLU 87 ) and (E GLN 93 ) are linked together, Residues (E ASN 190 ) and (E ILE 192 ) are linked together, Residues (E GLY 274 ) and (E GLY 291 ) are linked together, Residues (E ARG 312 ) and (E ALA 314 ) are linked together, Residues (F ASP 7 ) and (F ASN 11 ) are linked together, Residues (F ARG 168 ) and (F LEU 193 ) are linked together, Residues (F GLY 230 ) and (F ARG 231 ) are linked together, Residues (G GLY 107 ) and (G LEU 128 ) are linked together, Residues (K GLY 86 ) and (K ARG 88 ) are linked together, Residues (M PRO 88 ) and (M LYS 90 ) are linked together, Residues (O GLU 83 ) and (O ASP 92 ) are linked together, Residues (O VAL 96 ) and (O ALA 100 ) are linked together, Residues (Q THR 49 ) and (Q PRO 52 ) are linked together, Residues (Q GLU 72 ) and (Q PRO 74 ) are linked together, Residues (Q GLY 76 ) and (Q SER 80 ) are linked together, Residues (Q PRO 111 ) and (Q LYS 114 ) are linked together, Residues (R LEU 42 ) and (R ARG 44 ) are linked together, Residues (T PHE 20 ) and (T ASN 22 ) are linked together, Residues (T ASP 73 ) and (T GLN 75 ) are linked together, Residues (U GLY 36 ) and (U VAL 40 ) are linked together, Residues (W ARG 31 ) and (W VAL 33 ) are linked together. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4v4p.cif.gz | 3.7 MB | Display | PDBx/mmCIF format |
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PDB format | pdb4v4p.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 4v4p.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4v4p_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 4v4p_full_validation.pdf.gz | 5.3 MB | Display | |
Data in XML | 4v4p_validation.xml.gz | 981 KB | Display | |
Data in CIF | 4v4p_validation.cif.gz | 1.3 MB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v4/4v4p ftp://data.pdbj.org/pub/pdb/validation_reports/v4/4v4p | HTTPS FTP |
-Related structure data
Related structure data | 1ad2S 1bxeS 1bxyS 1gd8S 1giy 1nkwS 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, 6 molecules ABAABABBBCB1
#1: RNA chain | Mass: 39846.781 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / References: GenBank: 48271 | ||
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#2: RNA chain | Mass: 947975.500 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / References: GenBank: 48268 | ||
#34: RNA chain | Mass: 493958.281 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / Keywords: MONOMER / References: GenBank: 155076 | ||
#35: RNA chain | Mass: 24518.570 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / Keywords: MONOMER #36: RNA chain | | Mass: 24992.760 Da / Num. of mol.: 1 Fragment: nucleotides -59 to +19 of thrS mRNA (here renumbered 1 to 77) Source method: obtained synthetically Details: T7 transcript of the E.coli thrmRNA 78 nuc fragment Keywords: MONOMER |
+50S ribosomal protein ... , 30 types, 31 molecules ACADAEAFAGAHAIAJAKALAMANAOAPAQARASATAUAWAXA0A1A2A3A4A5A6A7A8A9
-Protein , 1 types, 1 molecules AV
#21: Protein | Mass: 27004.121 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 |
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-30S ribosomal protein ... , 20 types, 20 molecules BEBFBGBHBIBJBKBLBMBNBOBPBQBRBSBTBUBVBWBX
#37: Protein | Mass: 29317.703 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / Keywords: MONOMER / References: UniProt: P80371 |
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#38: Protein | Mass: 26751.076 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / Keywords: MONOMER / References: UniProt: Q5SHP4, UniProt: P80372*PLUS |
#39: Protein | Mass: 24373.447 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / Keywords: MONOMER / References: UniProt: Q5SHR5, UniProt: P80373*PLUS |
#40: Protein | Mass: 17583.416 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / Keywords: MONOMER / References: UniProt: Q5SHQ5 |
#41: Protein | Mass: 11988.753 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / Keywords: MONOMER / References: UniProt: Q5SLP8 |
#42: Protein | Mass: 18050.973 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / Keywords: MONOMER / References: UniProt: Q5SHN4, UniProt: P17291*PLUS |
#43: Protein | Mass: 15868.570 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / Keywords: MONOMER / References: UniProt: Q5SHQ2, UniProt: A0A0M9AFS9*PLUS |
#44: Protein | Mass: 14429.661 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / Keywords: MONOMER / References: UniProt: Q5SIB0, UniProt: P80374*PLUS |
#45: Protein | Mass: 11954.968 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / Keywords: MONOMER / References: UniProt: Q5SHN7 |
#46: Protein | Mass: 13737.868 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / Keywords: MONOMER / References: UniProt: P80376 |
#47: Protein | Mass: 14920.754 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Species: Thermus thermophilus / Strain: HB8 / ATCC 27634 / DSM 579 / Keywords: MONOMER / References: UniProt: Q5SHN3 |
#48: Protein | Mass: 14338.861 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / Keywords: MONOMER / References: UniProt: P80377 |
#49: Protein | Mass: 7158.725 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / Keywords: MONOMER / References: UniProt: Q5SHQ1, UniProt: A0A0N0BLP2*PLUS |
#50: Protein | Mass: 10578.407 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / Keywords: MONOMER / References: UniProt: Q5SJ76 |
#51: Protein | Mass: 10409.983 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / Keywords: MONOMER / References: UniProt: Q5SJH3 |
#52: Protein | Mass: 12324.670 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Species: Thermus thermophilus / Strain: HB8 / ATCC 27634 / DSM 579 / Keywords: MONOMER / References: UniProt: Q5SHP7, UniProt: A0A0N0BLS5*PLUS |
#53: Protein | Mass: 10244.272 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / Keywords: MONOMER / References: UniProt: Q5SLQ0 |
#54: Protein | Mass: 10605.464 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / Keywords: MONOMER / References: UniProt: Q5SHP2 |
#55: Protein | Mass: 11722.116 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / Keywords: MONOMER / References: UniProt: Q5SIH2, UniProt: P80380*PLUS |
#56: Protein/peptide | Mass: 3350.030 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / Keywords: MONOMER / References: UniProt: Q5SIH3 |
-Details
Has protein modification | Y |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 5.9 Å3/Da / Density % sol: 87.1 % | ||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: MPD, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||
Components of the solutions |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.97934 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: May 30, 2004 / Details: Dynamically Bendable Mirror |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97934 Å / Relative weight: 1 |
Reflection | Resolution: 5.5→300 Å / Num. obs: 165570 / % possible obs: 97.9 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 5.4 % / Rmerge(I) obs: 0.096 / Rsym value: 0.096 / Χ2: 1.047 / Net I/σ(I): 13.9 |
Reflection shell | Resolution: 5.5→5.59 Å / Redundancy: 4.2 % / Mean I/σ(I) obs: 1.83 / Num. unique all: 7889 / Χ2: 1.573 / % possible all: 94.2 |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS Starting model: PDB entries 1giy (70S ribosome), 1nkw (50S subunit of D. rad. ribosome), 1ad2, 1gd8, 1bxe, 1bxy (T. th. ribosomal proteins L1, L17, L22 and L30 Resolution: 5.5→300 Å / Data cutoff high absF: 10000 / Data cutoff low absF: 2 / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 204 Å2 | ||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 5.5→300 Å
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Refine LS restraints |
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LS refinement shell |
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