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- PDB-2npp: Structure of the Protein Phosphatase 2A Holoenzyme -

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Basic information

Entry
Database: PDB / ID: 2npp
TitleStructure of the Protein Phosphatase 2A Holoenzyme
Components
  • Protein Phosphatase 2, regulatory subunit A (PR 65), alpha isoform
  • Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform
  • Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
  • microcystin LRMicrocystin-LR
KeywordsHYDROLASE/HYDROLASE INHIBITOR / HEAT repeat / SIGNALING PROTEIN / HYDROLASE-HYDROLASE INHIBITOR COMPLEX
Function / homology
Function and homology information


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 ...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 / negative regulation of tyrosine phosphorylation of STAT protein / 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 / ceramide metabolic process / GABA receptor binding / negative regulation of epithelial to mesenchymal transition / 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 / 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 / Disassembly of the destruction complex and recruitment of AXIN to the membrane / regulation of Wnt signaling pathway / regulation of growth / negative regulation of glycolytic process through fructose-6-phosphate / positive regulation of NLRP3 inflammasome complex assembly / myosin phosphatase activity / protein serine/threonine phosphatase activity / CTLA4 inhibitory signaling / Platelet sensitization by LDL / negative regulation of MAPK cascade / protein-serine/threonine phosphatase / regulation of cell differentiation / T cell homeostasis / ERK/MAPK targets / protein phosphatase activator activity / regulation of G1/S transition of mitotic cell cycle / regulation of DNA replication / phosphoprotein phosphatase activity / mesoderm development / chromosome, centromeric region / DARPP-32 events / negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / lateral plasma membrane / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / regulation of cell adhesion / Cyclin A/B1/B2 associated events during G2/M transition / DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest / 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 / RNA splicing / meiotic cell cycle / response to organic substance / protein tyrosine phosphatase activity / chromosome segregation / RHO GTPases Activate Formins / response to lead ion / regulation of protein phosphorylation / Spry regulation of FGF signaling / RAF activation / tau protein binding / PKR-mediated signaling / Degradation of beta-catenin by the destruction complex / positive regulation of protein serine/threonine kinase activity / negative regulation of cell growth / spindle pole / Negative regulation of MAPK pathway / Separation of Sister Chromatids / Cyclin D associated events in G1 / microtubule cytoskeleton / Regulation of PLK1 Activity at G2/M Transition / Regulation of TP53 Degradation / mitotic cell cycle / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / proteasome-mediated ubiquitin-dependent protein catabolic process / protein-containing complex assembly / neuron projection
Similarity search - Function
Protein phosphatase 2A, regulatory B subunit, B56 / Protein phosphatase 2A regulatory B subunit (B56 family) / : / HEAT repeat / HEAT repeat / Serine/threonine specific protein phosphatases signature. / Protein phosphatase 2A homologues, catalytic domain. / Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase / HEAT repeat profile. / HEAT, type 2 ...Protein phosphatase 2A, regulatory B subunit, B56 / Protein phosphatase 2A regulatory B subunit (B56 family) / : / HEAT repeat / HEAT repeat / Serine/threonine specific protein phosphatases signature. / Protein phosphatase 2A homologues, catalytic domain. / Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase / HEAT repeat profile. / HEAT, type 2 / HEAT repeats / Metallo-dependent phosphatases / Purple Acid Phosphatase; chain A, domain 2 / Calcineurin-like phosphoesterase domain, ApaH type / Calcineurin-like phosphoesterase / Leucine-rich Repeat Variant / Leucine-rich Repeat Variant / Metallo-dependent phosphatase-like / Armadillo-like helical / 4-Layer Sandwich / Alpha Horseshoe / Armadillo-type fold / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Microcystin LR / : / : / Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform / Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform / Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform / Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
Similarity search - Component
Biological speciesHomo sapiens (human)
Cyanobacteria (blue-green algae)
MethodX-RAY DIFFRACTION / SYNCHROTRON / combined with Molecular Replacement / Resolution: 3.3 Å
AuthorsXu, Y. / Chen, Y. / Xing, Y. / Chao, Y. / Shi, Y.
CitationJournal: Cell(Cambridge,Mass.) / Year: 2006
Title: Structure of the protein phosphatase 2A holoenzyme
Authors: Xu, Y. / Xing, Y. / Chen, Y. / Chao, Y. / Lin, Z. / Fan, E. / Yu, J.W. / Strack, S. / Jeffrey, P.D. / Shi, Y.
History
DepositionOct 28, 2006Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 12, 2006Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jul 27, 2011Group: Database references / Derived calculations / Non-polymer description
Revision 1.4Feb 27, 2013Group: Other
Revision 2.0Nov 15, 2023Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations
Category: atom_site / chem_comp_atom ...atom_site / chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / pdbx_validate_main_chain_plane / pdbx_validate_peptide_omega / pdbx_validate_polymer_linkage / pdbx_validate_rmsd_angle / struct_conn / struct_conn_type / struct_ref_seq_dif / struct_site
Item: _atom_site.auth_atom_id / _atom_site.label_atom_id ..._atom_site.auth_atom_id / _atom_site.label_atom_id / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn_type.id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Protein Phosphatase 2, regulatory subunit A (PR 65), alpha isoform
B: Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform
C: Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
D: Protein Phosphatase 2, regulatory subunit A (PR 65), alpha isoform
E: Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform
F: Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
X: microcystin LR
Y: microcystin LR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)309,66812
Polymers309,4488
Non-polymers2204
Water0
1
D: Protein Phosphatase 2, regulatory subunit A (PR 65), alpha isoform
E: Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform
F: Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
Y: microcystin LR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)154,8346
Polymers154,7244
Non-polymers1102
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8950 Å2
ΔGint-18 kcal/mol
Surface area54380 Å2
MethodPISA
2
A: Protein Phosphatase 2, regulatory subunit A (PR 65), alpha isoform
B: Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform
C: Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
X: microcystin LR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)154,8346
Polymers154,7244
Non-polymers1102
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8940 Å2
ΔGint-18 kcal/mol
Surface area54450 Å2
MethodPISA
Unit cell
Length a, b, c (Å)109.260, 159.050, 269.170
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
DetailsThe complex exists as a hetero trimer

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Components

#1: Protein Protein Phosphatase 2, regulatory subunit A (PR 65), alpha isoform / / Protein Phosphatase 2A


Mass: 65378.344 Da / Num. of mol.: 2 / Fragment: scaffolding subunit
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PPP2R1A / Plasmid: pGEX-2T / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q96DH3, UniProt: P30153*PLUS
#2: Protein Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform / PP2A / B subunit / B' gamma isoform / PP2A / B subunit / B56 gamma isoform / PP2A / B subunit / ...PP2A / B subunit / B' gamma isoform / PP2A / B subunit / B56 gamma isoform / PP2A / B subunit / PR61 gamma isoform / PP2A / B subunit / R5 gamma isoform / NY-REN-29 antigen


Mass: 52695.270 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PPP2R5C, KIAA0044 / Plasmid: pGEX-2T / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q13362
#3: Protein Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform / E.C.3.1.3.16 / serine/threonine protein phosphatase / PP2A-alpha / Replication protein C / RP-C


Mass: 35636.152 Da / Num. of mol.: 2 / Fragment: catalytic subunit
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PPP2CA / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): Hi-5
References: UniProt: P67775, protein-serine/threonine phosphatase
#4: Protein/peptide microcystin LR / Microcystin-LR / Microcystin-LR


Type: Oligopeptide / Class: Toxin / Mass: 1014.195 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) Cyanobacteria (blue-green algae) / References: NOR: NOR00109, Microcystin LR
#5: Chemical
ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mn

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.78 Å3/Da / Density % sol: 67.44 %
Crystal growTemperature: 277.5 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: 15% PEG 8000, 0.1 M Tris-Cl pH 8.5, and 0.2 M magnesium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 277.5K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 0.9793 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Oct 9, 2006
RadiationMonochromator: a vertically focusing mirror and a horizontally focusing monochromator
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9793 Å / Relative weight: 1
ReflectionResolution: 3.3→100 Å / Num. all: 70359 / Num. obs: 70289 / % possible obs: 99.9 % / Observed criterion σ(I): 1 / Rmerge(I) obs: 0.104
Reflection shellResolution: 3.3→3.42 Å / % possible all: 99.9

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Processing

Software
NameClassification
CBASSdata collection
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling
CNSphasing
RefinementMethod to determine structure: combined with Molecular Replacement
Resolution: 3.3→100 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.299 66650 -Random
Rwork0.255 ---
all0.285 70359 --
obs0.26 70199 98.4 %-
Refinement stepCycle: LAST / Resolution: 3.3→100 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms20462 0 4 0 20466
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_bond_d0.0084
X-RAY DIFFRACTIONc_angle_deg1.38
X-RAY DIFFRACTIONc_mcbond_it2.8551.5
X-RAY DIFFRACTIONc_mcangle_it4.8352
X-RAY DIFFRACTIONc_scbond_it4.1482
X-RAY DIFFRACTIONc_scangle_it6.5222.5

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