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Yorodumi- PDB-2wjy: Crystal structure of the complex between human nonsense mediated ... -
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-Basic information
Entry | Database: PDB / ID: 2wjy | ||||||
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Title | Crystal structure of the complex between human nonsense mediated decay factors UPF1 and UPF2 Orthorhombic form | ||||||
Components | REGULATOR OF NONSENSE TRANSCRIPTS 1 | ||||||
Keywords | HYDROLASE / NONSENSE MEDIATED DECAY / ZINC-FINGER / ATP-BINDING / METAL-BINDING / UPF2 / UPF1 / HELICASE / NONSENSE-MEDIATED MRNA DECAY / PHOSPHOPROTEIN / NUCLEOTIDE-BINDING | ||||||
Function / homology | Function and homology information double-stranded DNA helicase activity / supraspliceosomal complex / positive regulation of mRNA cis splicing, via spliceosome / exon-exon junction complex / telomere maintenance via semi-conservative replication / positive regulation of mRNA catabolic process / cell cycle phase transition / regulation of translational termination / histone mRNA catabolic process / 3'-UTR-mediated mRNA destabilization ...double-stranded DNA helicase activity / supraspliceosomal complex / positive regulation of mRNA cis splicing, via spliceosome / exon-exon junction complex / telomere maintenance via semi-conservative replication / positive regulation of mRNA catabolic process / cell cycle phase transition / regulation of translational termination / histone mRNA catabolic process / 3'-UTR-mediated mRNA destabilization / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / regulation of telomere maintenance / DNA duplex unwinding / nuclear-transcribed mRNA catabolic process / telomeric DNA binding / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / cellular response to interleukin-1 / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / mRNA export from nucleus / helicase activity / P-body / cellular response to lipopolysaccharide / DNA replication / DNA helicase / chromosome, telomeric region / RNA helicase activity / RNA helicase / DNA repair / chromatin binding / protein-containing complex binding / chromatin / perinuclear region of cytoplasm / ATP hydrolysis activity / RNA binding / zinc ion binding / nucleoplasm / ATP binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Clerici, M. / Mourao, A. / Gutsche, I. / Gehring, N.H. / Hentze, M.W. / Kulozik, A. / Kadlec, J. / Sattler, M. / Cusack, S. | ||||||
Citation | Journal: Embo J. / Year: 2009 Title: Unusual Bipartite Mode of Interaction between the Nonsense-Mediated Decay Factors, Upf1 and Upf2. Authors: Clerici, M. / Mourao, A. / Gutsche, I. / Gehring, N.H. / Hentze, M.W. / Kulozik, A. / Kadlec, J. / Sattler, M. / Cusack, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2wjy.cif.gz | 171.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2wjy.ent.gz | 133.9 KB | Display | PDB format |
PDBx/mmJSON format | 2wjy.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2wjy_validation.pdf.gz | 445.2 KB | Display | wwPDB validaton report |
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Full document | 2wjy_full_validation.pdf.gz | 458.9 KB | Display | |
Data in XML | 2wjy_validation.xml.gz | 31.1 KB | Display | |
Data in CIF | 2wjy_validation.cif.gz | 44.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wj/2wjy ftp://data.pdbj.org/pub/pdb/validation_reports/wj/2wjy | HTTPS FTP |
-Related structure data
Related structure data | 2wjvC 2gk7S 2iykS C: citing same article (ref.) S: Starting model for refinement |
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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: 89984.242 Da / Num. of mol.: 1 / Fragment: CH-DOMAIN AND HELICASE DOMAIN, RESIDUES 115-914 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 STAR (DE3) References: UniProt: Q92900, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides | ||||||
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#2: Chemical | #3: Chemical | ChemComp-SO4 / #4: Water | ChemComp-HOH / | Nonpolymer details | SULPHATE ION (SO4): FROM CRSYTALLIS | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.23 Å3/Da / Density % sol: 62 % / Description: NONE |
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Crystal grow | pH: 6 Details: 1.6M AMMONIUM SULPHATE, 100 MM MES PH 6, 10% DIOXANE |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.976 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Mar 25, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.976 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→30 Å / Num. obs: 45136 / % possible obs: 98.4 % / Observed criterion σ(I): 0 / Redundancy: 3.71 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 11.2 |
Reflection shell | Resolution: 2.5→2.6 Å / Redundancy: 3.78 % / Rmerge(I) obs: 0.77 / Mean I/σ(I) obs: 1.9 / % possible all: 98 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRIES 2GK7, 2IYK Resolution: 2.5→46.52 Å / Cor.coef. Fo:Fc: 0.94 / Cor.coef. Fo:Fc free: 0.907 / SU B: 16.68 / SU ML: 0.17 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.308 / ESU R Free: 0.239 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES RESIDUAL ONLY
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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: 45.9 Å2
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Refinement step | Cycle: LAST / Resolution: 2.5→46.52 Å
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Refine LS restraints |
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