+Open data
-Basic information
Entry | Database: PDB / ID: 1tql | ||||||
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Title | POLIOVIRUS POLYMERASE G1A MUTANT | ||||||
Components | RNA-directed RNA polymeraseRNA-dependent RNA polymerase | ||||||
Keywords | TRANSFERASE / NUCLEOTIDYLTRANSFERASE / POLIOVIRUS / 3D / RNA-DEPENDENT / POLYMERASE / N-TERMINUS | ||||||
Function / homology | Function and homology information symbiont-mediated suppression of host translation initiation / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / ribonucleoside triphosphate phosphatase activity / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid ...symbiont-mediated suppression of host translation initiation / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / ribonucleoside triphosphate phosphatase activity / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / endocytosis involved in viral entry into host cell / : / nucleoside-triphosphate phosphatase / protein complex oligomerization / monoatomic ion channel activity / RNA helicase activity / induction by virus of host autophagy / RNA-directed RNA polymerase / symbiont-mediated suppression of host gene expression / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / DNA-templated transcription / host cell nucleus / virion attachment to host cell / structural molecule activity / proteolysis / RNA binding / ATP binding / membrane / metal ion binding Similarity search - Function | ||||||
Biological species | Human poliovirus 1 | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | Thompson, A.A. / Peersen, O.B. | ||||||
Citation | Journal: Embo J. / Year: 2004 Title: Structural basis for proteolysis-dependent activation of the poliovirus RNA-dependent RNA polymerase Authors: Thompson, A.A. / Peersen, O.B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1tql.cif.gz | 109 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1tql.ent.gz | 83.2 KB | Display | PDB format |
PDBx/mmJSON format | 1tql.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tq/1tql ftp://data.pdbj.org/pub/pdb/validation_reports/tq/1tql | HTTPS FTP |
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-Related structure data
Related structure data | 1ra6SC 1ra7C 1rajC 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: Protein | Mass: 53001.887 Da / Num. of mol.: 1 / Mutation: G1A, L446D, R455D Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human poliovirus 1 / Genus: Enterovirus / Species: Poliovirus / Gene: 3D / Plasmid: PKKT7E / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) PLYSS / References: UniProt: P03300, RNA-directed RNA polymerase | ||
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#2: Chemical | ChemComp-ACY / #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 5.04 Å3/Da / Density % sol: 75.58 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop / pH: 7 Details: sodium acetate, cacodylate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 4.2.2 / Wavelength: 0.98 Å |
Detector | Type: NOIR-1 / Detector: CCD / Date: Apr 21, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→30 Å / Num. all: 46651 / Num. obs: 46290 / % possible obs: 99.2 % / Redundancy: 6.04 % / Rmerge(I) obs: 0.074 / Net I/σ(I): 13.8 |
Reflection shell | Resolution: 2.3→2.38 Å / Redundancy: 4.39 % / Rmerge(I) obs: 0.504 / Mean I/σ(I) obs: 2.3 / Num. unique all: 4614 / % possible all: 96.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: pdb entry 1RA6 Resolution: 2.3→30 Å / Isotropic thermal model: ANISOTROPIC / Cross valid method: THROUGHOUT Details: the structure was refined with anomalous data to account for significant anomalous signal from arsenic, which is found in several CAS residues in the structure. However, the data reduction ...Details: the structure was refined with anomalous data to account for significant anomalous signal from arsenic, which is found in several CAS residues in the structure. However, the data reduction and completeness statistics are based on merging anomalous reflections.
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Displacement parameters | Biso mean: 62.1 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.3→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.3→2.38 Å / Rfactor Rfree error: 0.018
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