+Open data
-Basic information
Entry | Database: PDB / ID: 1fxl | ||||||
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Title | CRYSTAL STRUCTURE OF HUD AND AU-RICH ELEMENT OF THE C-FOS RNA | ||||||
Components |
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Keywords | TRANSCRIPTION/RNA / PROTEIN-RNA COMPLEX / HuD / AU-Rich Element / TRANSCRIPTION-RNA COMPLEX | ||||||
Function / homology | Function and homology information positive regulation of 3'-UTR-mediated mRNA stabilization / regeneration / pre-mRNA intronic pyrimidine-rich binding / regulation of translation at postsynapse / cerebral cortex neuron differentiation / apical dendrite / mRNA 3'-UTR AU-rich region binding / poly(A) binding / positive regulation of dendrite development / dendrite morphogenesis ...positive regulation of 3'-UTR-mediated mRNA stabilization / regeneration / pre-mRNA intronic pyrimidine-rich binding / regulation of translation at postsynapse / cerebral cortex neuron differentiation / apical dendrite / mRNA 3'-UTR AU-rich region binding / poly(A) binding / positive regulation of dendrite development / dendrite morphogenesis / 3'-UTR-mediated mRNA stabilization / associative learning / RNA processing / response to endoplasmic reticulum stress / RNA splicing / cellular response to nerve growth factor stimulus / response to cocaine / locomotory behavior / mRNA 3'-UTR binding / mRNA processing / nuclear envelope / growth cone / perikaryon / postsynapse / ribosome / ribonucleoprotein complex / axon / glutamatergic synapse / dendrite / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.8 Å | ||||||
Authors | Wang, X. / Hall, T.M.T. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 2001 Title: Structural basis for recognition of AU-rich element RNA by the HuD protein. Authors: Wang, X. / Tanaka Hall, T.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fxl.cif.gz | 54.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fxl.ent.gz | 38.3 KB | Display | PDB format |
PDBx/mmJSON format | 1fxl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fx/1fxl ftp://data.pdbj.org/pub/pdb/validation_reports/fx/1fxl | HTTPS FTP |
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-Related 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: 2733.574 Da / Num. of mol.: 1 / Fragment: FRAGMENT OF THE C-FOS AU-RICH ELEMENT / Source method: obtained synthetically |
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#2: Protein | Mass: 18547.186 Da / Num. of mol.: 1 / Fragment: N-TERMINAL TWO RRM-DOMAINS Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Organ: BRAIN / Plasmid: PPROEXHTC / Production host: Escherichia coli (E. coli) / References: UniProt: P26378 |
#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: 2.26 Å3/Da / Density % sol: 45.65 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: PEG 3350, Ammonium sulfate, Calcium chloride, Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K | ||||||||||||||||||||||||||||||
Components of the solutions |
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Crystal | *PLUS Density % sol: 43 % | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||
Radiation wavelength |
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Reflection | Resolution: 1.8→30.45 Å / Num. all: 16220 / Num. obs: 16220 / % possible obs: 92.3 % / Observed criterion σ(I): -3 / Redundancy: 4.3 % / Biso Wilson estimate: 19.2 Å2 / Rmerge(I) obs: 0.075 / Net I/σ(I): 12.8 | ||||||||||||||||||
Reflection shell | Resolution: 1.8→1.86 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.329 / Num. unique all: 1485 / % possible all: 85.1 | ||||||||||||||||||
Reflection | *PLUS | ||||||||||||||||||
Reflection shell | *PLUS Highest resolution: 1.8 Å / Mean I/σ(I) obs: 1.9 |
-Processing
Software |
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Refinement | Resolution: 1.8→30.45 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber Details: A final round of refinement was performed by using all data including reflections set aside for cross-validation in a "free" R-factor set. For last nucleotide U11, only the 5' phosphate group was observed.
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Refinement step | Cycle: LAST / Resolution: 1.8→30.45 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Version: 0.9 / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.8 Å / σ(F): 0 / % reflection Rfree: 6 % | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 25.1 Å2 | |||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: c_angle_deg / Dev ideal: 1.19 |