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Yorodumi- PDB-1xks: The crystal structure of the N-terminal domain of Nup133 reveals ... -
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-Basic information
Entry | Database: PDB / ID: 1xks | ||||||
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Title | The crystal structure of the N-terminal domain of Nup133 reveals a beta-propeller fold common to several nucleoporins | ||||||
Components | Nuclear pore complex protein Nup133 | ||||||
Keywords | PROTEIN TRANSPORT / beta-propeller / helical insertions | ||||||
Function / homology | Function and homology information nephron development / transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery / nuclear pore organization / nuclear pore outer ring / somite development / Nuclear Pore Complex (NPC) Disassembly / paraxial mesoderm development / Transport of Ribonucleoproteins into the Host Nucleus / Regulation of Glucokinase by Glucokinase Regulatory Protein / Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC) ...nephron development / transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery / nuclear pore organization / nuclear pore outer ring / somite development / Nuclear Pore Complex (NPC) Disassembly / paraxial mesoderm development / Transport of Ribonucleoproteins into the Host Nucleus / Regulation of Glucokinase by Glucokinase Regulatory Protein / Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC) / Transport of the SLBP independent Mature mRNA / Transport of the SLBP Dependant Mature mRNA / NS1 Mediated Effects on Host Pathways / SUMOylation of SUMOylation proteins / Transport of Mature mRNA Derived from an Intronless Transcript / structural constituent of nuclear pore / Rev-mediated nuclear export of HIV RNA / SUMOylation of RNA binding proteins / Nuclear import of Rev protein / Transport of Mature mRNA derived from an Intron-Containing Transcript / NEP/NS2 Interacts with the Cellular Export Machinery / tRNA processing in the nucleus / Postmitotic nuclear pore complex (NPC) reformation / neural tube development / poly(A)+ mRNA export from nucleus / nucleocytoplasmic transport / Viral Messenger RNA Synthesis / SUMOylation of ubiquitinylation proteins / Vpr-mediated nuclear import of PICs / SUMOylation of DNA replication proteins / Regulation of HSF1-mediated heat shock response / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / mRNA export from nucleus / SUMOylation of DNA damage response and repair proteins / nuclear pore / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / neurogenesis / SUMOylation of chromatin organization proteins / HCMV Late Events / RHO GTPases Activate Formins / Transcriptional regulation by small RNAs / kinetochore / ISG15 antiviral mechanism / HCMV Early Events / protein import into nucleus / Separation of Sister Chromatids / nuclear envelope / snRNP Assembly / nuclear membrane / SARS-CoV-2 activates/modulates innate and adaptive immune responses / membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.35 Å | ||||||
Authors | Berke, I.C. / Boehmer, T. / Blobel, G. / Schwartz, T.U. | ||||||
Citation | Journal: J.Cell Biol. / Year: 2004 Title: Structural and functional analysis of Nup133 domains reveals modular building blocks of the nuclear pore complex. Authors: Berke, I.C. / Boehmer, T. / Blobel, G. / Schwartz, T.U. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1xks.cif.gz | 89.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1xks.ent.gz | 66.9 KB | Display | PDB format |
PDBx/mmJSON format | 1xks.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xk/1xks ftp://data.pdbj.org/pub/pdb/validation_reports/xk/1xks | 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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-Components
#1: Protein | Mass: 48798.430 Da / Num. of mol.: 1 / Mutation: F345L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NUP133 / Plasmid: pET28 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 CodonPlus(DE3)-RIL / References: UniProt: Q8WUM0 |
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#2: 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: 2.6 Å3/Da / Density % sol: 51.5 % |
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Crystal grow | Temperature: 277 K / pH: 5.7 Details: PEG 3350, lithium sulfate, bis-tris, pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K, pH 5.70 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 8.2.1 / Wavelength: 1.0781 |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Jan 28, 2004 |
Radiation | Monochromator: DOUBLE CRYSTAL, SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0781 Å / Relative weight: 1 |
Reflection | Resolution: 2.35→40.5 Å / Num. obs: 20899 / % possible obs: 96.5 % / Observed criterion σ(I): 1 / Biso Wilson estimate: 71.03 Å2 |
Reflection shell | Resolution: 2.35→2.39 Å / % possible all: 93.2 |
-Processing
Software |
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Refinement | Method to determine structure: SAD Starting model: Model built by SAD data from SeMet derivative Resolution: 2.35→40.46 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.948 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.308 / ESU R Free: 0.227 / 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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 65.99 Å2
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Refinement step | Cycle: LAST / Resolution: 2.35→40.46 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.35→2.42 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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