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Yorodumi- PDB-1lj2: Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA c... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1lj2 | ||||||
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Title | Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization | ||||||
Components |
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Keywords | Viral protein/ translation / NSP3 / homodimer / eIF4G / Rotavirus / translation / mRNA / closed loop / coiled coil / Viral protein- translation COMPLEX | ||||||
Function / homology | Function and homology information positive regulation of eukaryotic translation initiation factor 4F complex assembly / positive regulation of mRNA cap binding / positive regulation of translation in response to endoplasmic reticulum stress / cap-dependent translational initiation / macromolecule biosynthetic process / Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S / eukaryotic initiation factor 4E binding / regulation of cellular response to stress / eukaryotic translation initiation factor 4F complex / Z-decay: degradation of maternal mRNAs by zygotically expressed factors ...positive regulation of eukaryotic translation initiation factor 4F complex assembly / positive regulation of mRNA cap binding / positive regulation of translation in response to endoplasmic reticulum stress / cap-dependent translational initiation / macromolecule biosynthetic process / Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S / eukaryotic initiation factor 4E binding / regulation of cellular response to stress / eukaryotic translation initiation factor 4F complex / Z-decay: degradation of maternal mRNAs by zygotically expressed factors / translation factor activity, RNA binding / Deadenylation of mRNA / miRNA-mediated gene silencing by inhibition of translation / M-decay: degradation of maternal mRNAs by maternally stored factors / positive regulation of protein localization to cell periphery / regulation of translational initiation / Ribosomal scanning and start codon recognition / Translation initiation complex formation / negative regulation of peptidyl-threonine phosphorylation / mTORC1-mediated signalling / cellular response to nutrient levels / regulation of presynapse assembly / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / GTP hydrolysis and joining of the 60S ribosomal subunit / L13a-mediated translational silencing of Ceruloplasmin expression / positive regulation of G1/S transition of mitotic cell cycle / behavioral fear response / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / energy homeostasis / translation initiation factor binding / translational initiation / positive regulation of neuron differentiation / positive regulation of protein metabolic process / translation initiation factor activity / negative regulation of autophagy / AUF1 (hnRNP D0) binds and destabilizes mRNA / lung development / ISG15 antiviral mechanism / neuron differentiation / Regulation of expression of SLITs and ROBOs / cytoplasmic stress granule / regulation of translation / positive regulation of peptidyl-serine phosphorylation / postsynapse / positive regulation of cell growth / response to ethanol / host cell cytoplasm / molecular adaptor activity / ribosome / translation / mRNA binding / RNA binding / ATP binding / membrane / identical protein binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Simian rotavirus A/SA11 | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.38 Å | ||||||
Authors | Groft, C.M. / Burley, S.K. | ||||||
Citation | Journal: Mol.Cell / Year: 2002 Title: Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization. Authors: Groft, C.M. / Burley, S.K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1lj2.cif.gz | 68.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lj2.ent.gz | 51.3 KB | Display | PDB format |
PDBx/mmJSON format | 1lj2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lj/1lj2 ftp://data.pdbj.org/pub/pdb/validation_reports/lj/1lj2 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | The assembly consists of an NSP3 homodimer bound to two fragments of eIF4G. |
-Components
#1: Protein | Mass: 12842.396 Da / Num. of mol.: 2 / Fragment: C-terminal domain / Mutation: C306S C314S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Simian rotavirus A/SA11 / Species: Rotavirus A / Production host: Escherichia coli (E. coli) / References: UniProt: P03536 #2: Protein/peptide | Mass: 3203.653 Da / Num. of mol.: 2 / Fragment: residues 132-159 of AAC82471 / Source method: obtained synthetically / Details: sequence appear naturally in Homo sapiens / References: UniProt: Q04637 #3: Chemical | #4: Water | ChemComp-HOH / | |
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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: 2.67 Å3/Da / Density % sol: 53.88 % | |||||||||||||||||||||||||
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Crystal grow | Temperature: 275 K / Method: vapor diffusion, hanging drop Details: PEG-MME 550, glucose, theophylline, unbuffered, VAPOR DIFFUSION, HANGING DROP at 275K | |||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X9A / Wavelength: 1.0447 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Aug 1, 2001 |
Radiation | Monochromator: crystal / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0447 Å / Relative weight: 1 |
Reflection | Resolution: 2.38→20 Å / Num. all: 26535 / Num. obs: 24286 / % possible obs: 99.9 % / Observed criterion σ(I): 1 |
Reflection shell | Resolution: 2.38→2.46 Å / % possible all: 99.9 |
Reflection | *PLUS Num. obs: 26797 / Num. measured all: 110178 / Rmerge(I) obs: 0.074 |
Reflection shell | *PLUS % possible obs: 99.9 % / Rmerge(I) obs: 0.316 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.38→20 Å / Cross valid method: THROUGHOUT / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.38→20 Å
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Refine LS restraints |
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Refinement | *PLUS % reflection Rfree: 7 % | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: c_angle_deg / Dev ideal: 1.01 |