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Yorodumi- PDB-4ed5: Crystal structure of the two N-terminal RRM domains of HuR comple... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4ed5 | ||||||
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Title | Crystal structure of the two N-terminal RRM domains of HuR complexed with RNA | ||||||
Components |
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Keywords | RNA BINDING PROTEIN/RNA / RRM / RNA binding / Nucleus / RNA BINDING PROTEIN-RNA complex | ||||||
Function / homology | Function and homology information HuR (ELAVL1) binds and stabilizes mRNA / negative regulation of miRNA-mediated gene silencing / post-transcriptional gene silencing / regulation of stem cell population maintenance / mRNA 3'-UTR AU-rich region binding / mRNA stabilization / lncRNA binding / miRNA binding / 3'-UTR-mediated mRNA stabilization / mRNA destabilization ...HuR (ELAVL1) binds and stabilizes mRNA / negative regulation of miRNA-mediated gene silencing / post-transcriptional gene silencing / regulation of stem cell population maintenance / mRNA 3'-UTR AU-rich region binding / mRNA stabilization / lncRNA binding / miRNA binding / 3'-UTR-mediated mRNA stabilization / mRNA destabilization / sarcoplasm / positive regulation of superoxide anion generation / mRNA 3'-UTR binding / positive regulation of translation / P-body / protein homooligomerization / cytoplasmic stress granule / protein import into nucleus / double-stranded RNA binding / cytoplasmic vesicle / postsynapse / ribonucleoprotein complex / mRNA binding / glutamatergic synapse / protein kinase binding / endoplasmic reticulum / protein homodimerization activity / RNA binding / nucleoplasm / membrane / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Wang, H. / Zeng, F. / Liu, Q. / Niu, L. / Teng, M. / Li, X. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2013 Title: The structure of the ARE-binding domains of Hu antigen R (HuR) undergoes conformational changes during RNA binding. Authors: Wang, H. / Zeng, F. / Liu, Q. / Liu, H. / Liu, Z. / Niu, L. / Teng, M. / Li, X. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4ed5.cif.gz | 163.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4ed5.ent.gz | 127.9 KB | Display | PDB format |
PDBx/mmJSON format | 4ed5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ed/4ed5 ftp://data.pdbj.org/pub/pdb/validation_reports/ed/4ed5 | 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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2 |
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Unit cell |
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-Components
-Protein / RNA chain , 2 types, 4 molecules ABCD
#1: Protein | Mass: 19812.375 Da / Num. of mol.: 2 / Fragment: RRM1/RRM2 domains, UNP RESIDUES 18-186 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ELAVL1, HUR / Production host: Escherichia coli (E. coli) / References: UniProt: Q15717 #2: RNA chain | Mass: 3368.946 Da / Num. of mol.: 2 / Source method: obtained synthetically |
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-Non-polymers , 4 types, 262 molecules
#3: Chemical | ChemComp-GOL / #4: Chemical | ChemComp-M2M / | #5: Chemical | #6: 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: 2.29 Å3/Da / Density % sol: 46.25 % |
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Crystal grow | Temperature: 287 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 18% PEG 5000, 0.1M HEPES, pH7.5, VAPOR DIFFUSION, HANGING DROP, temperature 287K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH3R / Wavelength: 0.9793 Å |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Mar 19, 2012 |
Radiation | Monochromator: Ni FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9793 Å / Relative weight: 1 |
Reflection | Resolution: 2→35.08 Å / Num. all: 28267 / Num. obs: 27777 / % possible obs: 98.3 % |
Reflection shell | Resolution: 2→2.11 Å / Rmerge(I) obs: 0.19 / Mean I/σ(I) obs: 4.8 / Rsym value: 0.226 / % possible all: 98.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→35.08 Å / Cor.coef. Fo:Fc: 0.925 / Cor.coef. Fo:Fc free: 0.884 / SU B: 10.318 / SU ML: 0.131 / Cross valid method: THROUGHOUT / ESU R: 0.209 / ESU R Free: 0.184 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 22.901 Å2
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Refinement step | Cycle: LAST / Resolution: 2→35.08 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.004→2.056 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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