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Yorodumi- PDB-5f5h: X-ray structure of Roquin ROQ domain in complex with Ox40 hexa-lo... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5f5h | ||||||
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Title | X-ray structure of Roquin ROQ domain in complex with Ox40 hexa-loop RNA motif | ||||||
Components |
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Keywords | RNA BINDING PROTEIN / ROQ domain / winged-helix domain / Ox40 mRNA | ||||||
Function / homology | Function and homology information negative regulation of germinal center formation / negative regulation of T-helper cell differentiation / regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / CCR4-NOT complex binding / regulation of T cell receptor signaling pathway / regulation of miRNA metabolic process / T follicular helper cell differentiation / positive regulation of mRNA catabolic process / negative regulation of T-helper 17 cell differentiation / regulation of germinal center formation ...negative regulation of germinal center formation / negative regulation of T-helper cell differentiation / regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / CCR4-NOT complex binding / regulation of T cell receptor signaling pathway / regulation of miRNA metabolic process / T follicular helper cell differentiation / positive regulation of mRNA catabolic process / negative regulation of T-helper 17 cell differentiation / regulation of germinal center formation / 3'-UTR-mediated mRNA destabilization / P-body assembly / RNA stem-loop binding / miRNA binding / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / nuclear-transcribed mRNA catabolic process / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / post-transcriptional regulation of gene expression / negative regulation of B cell proliferation / T cell homeostasis / negative regulation of activated T cell proliferation / B cell homeostasis / lymph node development / cellular response to interleukin-1 / T cell proliferation / spleen development / regulation of mRNA stability / mRNA 3'-UTR binding / P-body / RING-type E3 ubiquitin transferase / cytoplasmic stress granule / protein polyubiquitination / positive regulation of non-canonical NF-kappaB signal transduction / ubiquitin-protein transferase activity / ubiquitin protein ligase activity / double-stranded RNA binding / T cell receptor signaling pathway / ubiquitin-dependent protein catabolic process / regulation of gene expression / mRNA binding / zinc ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.23 Å | ||||||
Authors | Janowski, R. / Schlundt, A. / Sattler, M. / Niessing, D. | ||||||
Citation | Journal: Nat Commun / Year: 2016 Title: Roquin recognizes a non-canonical hexaloop structure in the 3'-UTR of Ox40. Authors: Janowski, R. / Heinz, G.A. / Schlundt, A. / Wommelsdorf, N. / Brenner, S. / Gruber, A.R. / Blank, M. / Buch, T. / Buhmann, R. / Zavolan, M. / Niessing, D. / Heissmeyer, V. / Sattler, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5f5h.cif.gz | 182.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5f5h.ent.gz | 143 KB | Display | PDB format |
PDBx/mmJSON format | 5f5h.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f5/5f5h ftp://data.pdbj.org/pub/pdb/validation_reports/f5/5f5h | HTTPS FTP |
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-Related structure data
Related structure data | 5f5fC 4qi0S 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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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 20528.561 Da / Num. of mol.: 2 / Fragment: ROQ domain, UNP residues 147-326 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Rc3h1, Gm551, Kiaa2025 / Production host: Escherichia coli (E. coli) / References: UniProt: Q4VGL6 #2: RNA chain | Mass: 6987.163 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Production host: Mus musculus (house mouse) #3: Chemical | ChemComp-GOL / | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.01 Å3/Da / Density % sol: 38.79 % |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, hanging drop / Details: PEG 3350, NaCl, Bis-TRIS / PH range: 5.5-6.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 1.25363 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Apr 8, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.25363 Å / Relative weight: 1 |
Reflection | Resolution: 2.23→50 Å / Num. obs: 21018 / % possible obs: 98.7 % / Redundancy: 3.9 % / Rmerge(I) obs: 0.059 / Net I/σ(I): 14.9 |
Reflection shell | Resolution: 2.23→2.29 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.683 / Mean I/σ(I) obs: 2.1 / % possible all: 97.7 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4QI0 Resolution: 2.23→50 Å / Cor.coef. Fo:Fc: 0.95 / Cor.coef. Fo:Fc free: 0.912 / SU B: 16.735 / SU ML: 0.196 / Cross valid method: THROUGHOUT / ESU R: 0.333 / ESU R Free: 0.235 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 52.263 Å2
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Refinement step | Cycle: 1 / Resolution: 2.23→50 Å
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