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Yorodumi- PDB-3q1q: Structure of a Bacterial Ribonuclease P Holoenzyme in Complex wit... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3q1q | |||||||||
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Title | Structure of a Bacterial Ribonuclease P Holoenzyme in Complex with tRNA | |||||||||
Components |
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Keywords | HYDROLASE/RNA / RNase P / ribozyme / ribonuclease P / tRNA / pre-tRNA / tetraloop-receptor / ribose zipper / a-minor interaction / base stacking / intermolecular base pairs / intermolecular RNA-RNA contacts / RNP / ribonucleoprotein complex / enzyme-product complex / metalloenzyme / RNA-metal interactions / shape complementarity / hydrolase-RNA complex / endonuclease | |||||||||
Function / homology | Function and homology information 3'-tRNA processing endoribonuclease activity / ribonuclease P complex / ribonuclease P / ribonuclease P activity / tRNA 5'-leader removal / tRNA binding Similarity search - Function | |||||||||
Biological species | Thermotoga maritima (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIRAS / Resolution: 3.8 Å | |||||||||
Authors | Reiter, N.J. / Osterman, A. / Torres-Larios, A. / Swinger, K.K. / Pan, T. / Mondragon, A. | |||||||||
Citation | Journal: Nature / Year: 2010 Title: Structure of a Bacterial Ribonuclease P Holoenzyme in Complex with tRNA. Authors: Reiter, N.J. / Osterman, A. / Torres-Larios, A. / Swinger, K.K. / Pan, T. / Mondragon, A. | |||||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3q1q.cif.gz | 239.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3q1q.ent.gz | 175 KB | Display | PDB format |
PDBx/mmJSON format | 3q1q.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q1/3q1q ftp://data.pdbj.org/pub/pdb/validation_reports/q1/3q1q | HTTPS FTP |
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-Related structure data
Related structure data | 3q1rC 1ehzS 1nz0S 2a2eS 2a64S S: Starting model for refinement C: citing same article (ref.) |
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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
#1: RNA chain | Mass: 112622.805 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: THE RNA WAS PREPARED BY IN VITRO TRANSCRIPTION | ||
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#2: Protein | Mass: 14363.003 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermotoga maritima (bacteria) / Gene: rnpA, RNPA OR TM1463, RNPB, TM_1463 / Plasmid: PGEX4T-2 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) PLYSS / References: UniProt: Q9X1H4, ribonuclease P | ||
#3: RNA chain | Mass: 27658.418 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: THE RNA WAS PREPARED BY IN VITRO TRANSCRIPTION | ||
#4: Chemical | ChemComp-MG / #5: Chemical | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 4.95 Å3/Da / Density % sol: 75.14 % Description: DUE TO THE ANISOTROPIC NATURE OF THE DIFFRACTION, THE DATA WERE TREATED IN TWO DIFFERENT WAYS: 1) BY APPLYING AN ANISOTROPIC CORRECTION TO THE DATA (ANISOTROPIC), AND 2) WITHOUT ANY ...Description: DUE TO THE ANISOTROPIC NATURE OF THE DIFFRACTION, THE DATA WERE TREATED IN TWO DIFFERENT WAYS: 1) BY APPLYING AN ANISOTROPIC CORRECTION TO THE DATA (ANISOTROPIC), AND 2) WITHOUT ANY ANISOTROPY CORRECTION (ISOTROPIC). WHILE COMPLETENESS OF THE HIGHEST RESOLUTION SHELL MAY APPEAR OF POOR QUALITY IN THE ANISOTROPIC CASE, THE DATA COLLECTION STATISTICS AND RWORK AND RFREE REFINEMENT STATISTICS WERE ACTUALLY BETTER FOR THE CARVED (ANISOTROPIC) DATA SET THAN FOR THE ISOTROPIC CASE. FOR THIS REASON, THE REPORTED 3Q1Q STRUCTURE AND HEADER REMARKS REFLECT THE CARVED, ANISOTROPICALLY CORRECTED DATA. |
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 6 Details: 1.8M Lithium sulfate, 0.05M sodium cacodylate, pH 6.0, VAPOR DIFFUSION, HANGING DROP |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 |
Detector | Type: RAYONIX MX-225 / Detector: CCD / Date: Feb 20, 2009 / Details: MIRRORS |
Radiation | Monochromator: DIAMOND LAUE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97872 Å / Relative weight: 1 |
Reflection | Resolution: 3.8→30 Å / Num. obs: 27116 / % possible obs: 88.5 % / Observed criterion σ(I): 3 / Redundancy: 5 % / Biso Wilson estimate: 129.78 Å2 / Rmerge(I) obs: 0.079 / Rsym value: 0.096 / Net I/σ(I): 12.2 |
Reflection shell | Resolution: 3.8→3.97 Å / Redundancy: 4.5 % / Rmerge(I) obs: 0.359 / Mean I/σ(I) obs: 3.2 / Rsym value: 0.432 / % possible all: 22.3 |
-Processing
Software |
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Refinement | Method to determine structure: MIRAS Starting model: 2A2E, 2A64, 1NZ0, 1EHZ Resolution: 3.8→28.97 Å / Cor.coef. Fo:Fc: 0.877 / Cor.coef. Fo:Fc free: 0.846 / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 80.04 Å2
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Refine analyze | Luzzati coordinate error obs: 0.87 Å | ||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.8→28.97 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.8→3.94 Å / Total num. of bins used: 14
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