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- PDB-4i5n: Structural mechanism of trimeric PP2A holoenzyme involving PR70: ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4i5n | |||||||||
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Title | Structural mechanism of trimeric PP2A holoenzyme involving PR70: insight for Cdc6 dephosphorylation | |||||||||
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![]() | HYDROLASE/TOXIN / EF Hand / Phosphatase / CDC6 (Substrate) / TRANSFERASE-TOXIN complex / HYDROLASE-TOXIN complex | |||||||||
Function / homology | ![]() cellular response to vasopressin / positive regulation of chromosome segregation / CDC6 association with the ORC:origin complex / meiotic spindle elongation / Integration of energy metabolism / PP2A-mediated dephosphorylation of key metabolic factors / regulation of microtubule binding / MASTL Facilitates Mitotic Progression / mitotic sister chromatid separation / regulation of meiotic cell cycle process involved in oocyte maturation ...cellular response to vasopressin / positive regulation of chromosome segregation / CDC6 association with the ORC:origin complex / meiotic spindle elongation / Integration of energy metabolism / PP2A-mediated dephosphorylation of key metabolic factors / regulation of microtubule binding / MASTL Facilitates Mitotic Progression / mitotic sister chromatid separation / regulation of meiotic cell cycle process involved in oocyte maturation / protein phosphatase type 2A complex / meiotic sister chromatid cohesion, centromeric / peptidyl-serine dephosphorylation / peptidyl-threonine dephosphorylation / positive regulation of microtubule binding / Regulation of glycolysis by fructose 2,6-bisphosphate metabolism / Inhibition of replication initiation of damaged DNA by RB1/E2F1 / female meiotic nuclear division / protein antigen binding / protein phosphatase regulator activity / GABA receptor binding / traversing start control point of mitotic cell cycle / DNA replication checkpoint signaling / APC truncation mutants have impaired AXIN binding / AXIN missense mutants destabilize the destruction complex / Truncations of AMER1 destabilize the destruction complex / Initiation of Nuclear Envelope (NE) Reformation / ERKs are inactivated / Transcription of E2F targets under negative control by DREAM complex / positive regulation of extrinsic apoptotic signaling pathway in absence of ligand / Beta-catenin phosphorylation cascade / Signaling by GSK3beta mutants / CTNNB1 S33 mutants aren't phosphorylated / CTNNB1 S37 mutants aren't phosphorylated / CTNNB1 S45 mutants aren't phosphorylated / CTNNB1 T41 mutants aren't phosphorylated / negative regulation of epithelial to mesenchymal transition / mitotic DNA replication checkpoint signaling / cellular response to angiotensin / regulation of mitotic metaphase/anaphase transition / regulation of growth / Disassembly of the destruction complex and recruitment of AXIN to the membrane / negative regulation of glycolytic process through fructose-6-phosphate / positive regulation of NLRP3 inflammasome complex assembly / myosin phosphatase activity / intercellular bridge / regulation of cyclin-dependent protein serine/threonine kinase activity / CTLA4 inhibitory signaling / protein serine/threonine phosphatase activity / Platelet sensitization by LDL / G1/S-Specific Transcription / negative regulation of DNA replication / protein-serine/threonine phosphatase / regulation of cell differentiation / ERK/MAPK targets / positive regulation of cytokinesis / T cell homeostasis / regulation of G1/S transition of mitotic cell cycle / DNA replication origin binding / mesoderm development / phosphoprotein phosphatase activity / chromosome, centromeric region / DARPP-32 events / lateral plasma membrane / Activation of the pre-replicative complex / DNA replication initiation / negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / spindle midzone / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Activation of ATR in response to replication stress / Cyclin A/B1/B2 associated events during G2/M transition / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / Resolution of Sister Chromatid Cohesion / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / protein dephosphorylation / meiotic cell cycle / protein tyrosine phosphatase activity / chromosome segregation / Assembly of the pre-replicative complex / RHO GTPases Activate Formins / response to lead ion / Spry regulation of FGF signaling / RAF activation / regulation of protein phosphorylation / Degradation of beta-catenin by the destruction complex / PKR-mediated signaling / tau protein binding / positive regulation of protein serine/threonine kinase activity / mitotic spindle / CDK-mediated phosphorylation and removal of Cdc6 / kinase binding / spindle pole / Orc1 removal from chromatin Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Wlodarchak, N. / Satyshur, K.A. / Guo, F. / Xing, Y. | |||||||||
![]() | ![]() Title: Structure of the Ca(2+)-dependent PP2A heterotrimer and insights into Cdc6 dephosphorylation. Authors: Wlodarchak, N. / Guo, F. / Satyshur, K.A. / Jiang, L. / Jeffrey, P.D. / Sun, T. / Stanevich, V. / Mumby, M.C. / Xing, Y. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 505.7 KB | Display | ![]() |
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PDB format | ![]() | 408.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 503.3 KB | Display | ![]() |
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Full document | ![]() | 537.9 KB | Display | |
Data in XML | ![]() | 83.5 KB | Display | |
Data in CIF | ![]() | 115.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
-Serine/threonine-protein phosphatase 2A ... , 3 types, 6 molecules ADBECF
#1: Protein | Mass: 65563.461 Da / Num. of mol.: 2 / Fragment: PP2A A alpha subunit (9-589) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | Mass: 47649.289 Da / Num. of mol.: 2 Fragment: UNP Q9Y5P8 residues 122-490 and UNP Q99741 residues 70-90 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Protein | Mass: 35780.281 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P67775, protein-serine/threonine phosphatase |
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-Protein/peptide , 1 types, 2 molecules GH
#4: Protein/peptide |
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-Non-polymers , 3 types, 181 molecules ![](data/chem/img/CA.gif)
![](data/chem/img/MN.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/MN.gif)
![](data/chem/img/HOH.gif)
#5: Chemical | ChemComp-CA / #6: Chemical | ChemComp-MN / #7: Water | ChemComp-HOH / | |
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-Details
Sequence details | THE LINKER IS DERIVED FROM JMJD6 |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.77 Å3/Da / Density % sol: 55.64 % |
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Crystal grow | Temperature: 296 K / Method: vapor diffusion, hanging drop / pH: 4.75 Details: 0.03M Succinic acid with 7% PEG 3350. Protein (6.2mg/mL) in 10mM tris pH 8.0, 150mM NaCl, 5mM DTT, 1mM CaCl2, VAPOR DIFFUSION, HANGING DROP, temperature 296K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Nov 5, 2011 |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97987 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→100 Å / Num. all: 119018 / Num. obs: 119018 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7.3 % / Rsym value: 0.157 / Net I/σ(I): 11.85 |
Reflection shell | Resolution: 2.5→2.54 Å / Redundancy: 4.8 % / % possible all: 99 |
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Processing
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Refinement | Method to determine structure: ![]()
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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: 54.432 Å2
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Refinement step | Cycle: LAST / Resolution: 2.8→49.08 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.8→2.873 Å / Total num. of bins used: 20
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