+Open data
-Basic information
Entry | Database: PDB / ID: 2i46 | ||||||
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Title | Crystal structure of human TPP1 | ||||||
Components | Adrenocortical dysplasia protein homolog | ||||||
Keywords | PROTEIN BINDING / TPP1 / OB fold / POT1 binding | ||||||
Function / homology | Function and homology information positive regulation of single-stranded telomeric DNA binding / telomere assembly / segmentation / urogenital system development / protection from non-homologous end joining at telomere / establishment of protein localization to telomere / shelterin complex / Telomere C-strand synthesis initiation / Telomere C-strand (Lagging Strand) Synthesis / Processive synthesis on the C-strand of the telomere ...positive regulation of single-stranded telomeric DNA binding / telomere assembly / segmentation / urogenital system development / protection from non-homologous end joining at telomere / establishment of protein localization to telomere / shelterin complex / Telomere C-strand synthesis initiation / Telomere C-strand (Lagging Strand) Synthesis / Processive synthesis on the C-strand of the telomere / nuclear telomere cap complex / positive regulation of telomere maintenance / Polymerase switching on the C-strand of the telomere / Removal of the Flap Intermediate from the C-strand / telomerase holoenzyme complex / telomere capping / embryonic limb morphogenesis / protein localization to chromosome, telomeric region / telomeric DNA binding / negative regulation of telomere maintenance via telomerase / Telomere Extension By Telomerase / telomere maintenance via telomerase / DNA polymerase binding / Packaging Of Telomere Ends / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / positive regulation of telomerase activity / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / positive regulation of telomere maintenance via telomerase / Inhibition of DNA recombination at telomere / Meiotic synapsis / telomere maintenance / skeletal system development / intracellular protein transport / DNA Damage/Telomere Stress Induced Senescence / chromosome, telomeric region / nuclear body / protein-containing complex binding / nucleoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.7 Å | ||||||
Authors | Wang, F. / Podell, E.R. / Zaug, A.J. / Yang, Y.T. / Baciu, P. / Else, T. / Hammer, G.D. / Cech, T.R. / Lei, M. | ||||||
Citation | Journal: Nature / Year: 2007 Title: The POT1-TPP1 telomere complex is a telomerase processivity factor. Authors: Wang, F. / Podell, E.R. / Zaug, A.J. / Yang, Y. / Baciu, P. / Cech, T.R. / Lei, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2i46.cif.gz | 68 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2i46.ent.gz | 51.3 KB | Display | PDB format |
PDBx/mmJSON format | 2i46.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i4/2i46 ftp://data.pdbj.org/pub/pdb/validation_reports/i4/2i46 | 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 on special symmetry positions |
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-Components
#1: Protein | Mass: 17558.533 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ACD, PIP1, PTOP / Plasmid: pET28b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: Q96AP0 #2: 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: 4.2 Å3/Da / Density % sol: 70.68 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: 3.5 M Sodium formate, 0.1 M sodium citrate, pH 5.6, 10 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 0.9795 Å |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Mar 15, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→50 Å / Num. all: 17184 / Num. obs: 16372 / % possible obs: 92.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 9.8 % / Biso Wilson estimate: 63.3 Å2 / Rmerge(I) obs: 0.116 / Net I/σ(I): 2.7 |
Reflection shell | Resolution: 2.7→2.8 Å / Rmerge(I) obs: 0.385 / Mean I/σ(I) obs: 4.3 / % possible all: 81.7 |
-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 2.7→50 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.7→50 Å
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Refine LS restraints |
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