[English] 日本語
Yorodumi
- PDB-5mx5: Mouse PA28alpha-beta -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5mx5
TitleMouse PA28alpha-beta
Components
  • Proteasome activator complex subunit 1
  • Proteasome activator complex subunit 2
KeywordsSTRUCTURAL PROTEIN / proteasome activator / regulator / heptamer / interferon-gamma / hydrolase
Function / homology
Function and homology information


Regulation of ornithine decarboxylase (ODC) / Cross-presentation of soluble exogenous antigens (endosomes) / proteasome activator complex / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Ubiquitin-dependent degradation of Cyclin D / AUF1 (hnRNP D0) binds and destabilizes mRNA / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / SCF(Skp2)-mediated degradation of p27/p21 ...Regulation of ornithine decarboxylase (ODC) / Cross-presentation of soluble exogenous antigens (endosomes) / proteasome activator complex / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Ubiquitin-dependent degradation of Cyclin D / AUF1 (hnRNP D0) binds and destabilizes mRNA / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / SCF(Skp2)-mediated degradation of p27/p21 / Assembly of the pre-replicative complex / CDK-mediated phosphorylation and removal of Cdc6 / Degradation of AXIN / Autodegradation of the E3 ubiquitin ligase COP1 / G2/M Checkpoints / Asymmetric localization of PCP proteins / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / Regulation of RUNX3 expression and activity / Regulation of RAS by GAPs / Regulation of PTEN stability and activity / Regulation of RUNX2 expression and activity / Degradation of GLI1 by the proteasome / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / Degradation of DVL / UCH proteinases / Orc1 removal from chromatin / Dectin-1 mediated noncanonical NF-kB signaling / NIK-->noncanonical NF-kB signaling / Hedgehog ligand biogenesis / TNFR2 non-canonical NF-kB pathway / positive regulation of endopeptidase activity / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Hedgehog 'on' state / antigen processing and presentation of exogenous antigen / Degradation of beta-catenin by the destruction complex / Activation of NF-kappaB in B cells / The role of GTSE1 in G2/M progression after G2 checkpoint / FCERI mediated NF-kB activation / CLEC7A (Dectin-1) signaling / Interleukin-1 signaling / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Separation of Sister Chromatids / Downstream TCR signaling / KEAP1-NFE2L2 pathway / MAPK6/MAPK4 signaling / GLI3 is processed to GLI3R by the proteasome / ABC-family proteins mediated transport / Neddylation / Antigen processing: Ubiquitination & Proteasome degradation / Ub-specific processing proteases / regulation of G1/S transition of mitotic cell cycle / endopeptidase activator activity / regulation of proteasomal protein catabolic process / nucleoplasm / identical protein binding / cytoplasm
Similarity search - Function
Proteasome activator PA28, N-terminal domain / Proteasome activator PA28, N-terminal domain superfamily / Proteasome activator pa28 alpha subunit / Proteasome activator PA28 / Proteasome activator PA28, C-terminal domain / Proteasome activator superfamily / Proteasome activator PA28, C-terminal domain superfamily / Proteasome activator pa28 beta subunit
Similarity search - Domain/homology
PHOSPHATE ION / Proteasome activator complex subunit 1 / Proteasome activator complex subunit 2
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.9 Å
AuthorsHuber, E.M. / Groll, M.
Funding support Germany, 1items
OrganizationGrant numberCountry
German Research FoundationSFB1035 Germany
CitationJournal: Structure / Year: 2017
Title: The Mammalian Proteasome Activator PA28 Forms an Asymmetric alpha 4 beta 3 Complex.
Authors: Huber, E.M. / Groll, M.
History
DepositionJan 20, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 13, 2017Provider: repository / Type: Initial release
Revision 1.1Oct 18, 2017Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.2Jan 17, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Proteasome activator complex subunit 1
B: Proteasome activator complex subunit 2
C: Proteasome activator complex subunit 1
D: Proteasome activator complex subunit 2
E: Proteasome activator complex subunit 1
F: Proteasome activator complex subunit 2
G: Proteasome activator complex subunit 1
H: Proteasome activator complex subunit 1
I: Proteasome activator complex subunit 2
J: Proteasome activator complex subunit 1
K: Proteasome activator complex subunit 2
L: Proteasome activator complex subunit 1
M: Proteasome activator complex subunit 2
N: Proteasome activator complex subunit 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)392,59417
Polymers392,30914
Non-polymers2853
Water4,432246
1
A: Proteasome activator complex subunit 1
B: Proteasome activator complex subunit 2
C: Proteasome activator complex subunit 1
D: Proteasome activator complex subunit 2
E: Proteasome activator complex subunit 1
F: Proteasome activator complex subunit 2
G: Proteasome activator complex subunit 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)196,3459
Polymers196,1557
Non-polymers1902
Water1267
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area27950 Å2
ΔGint-171 kcal/mol
Surface area64670 Å2
MethodPISA
2
H: Proteasome activator complex subunit 1
I: Proteasome activator complex subunit 2
J: Proteasome activator complex subunit 1
K: Proteasome activator complex subunit 2
L: Proteasome activator complex subunit 1
M: Proteasome activator complex subunit 2
N: Proteasome activator complex subunit 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)196,2508
Polymers196,1557
Non-polymers951
Water1267
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area25780 Å2
ΔGint-149 kcal/mol
Surface area63410 Å2
MethodPISA
Unit cell
Length a, b, c (Å)126.090, 137.380, 136.420
Angle α, β, γ (deg.)90.00, 104.44, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

#1: Protein
Proteasome activator complex subunit 1 / 11S regulator complex subunit alpha / REG-alpha / Activator of multicatalytic protease subunit 1 / ...11S regulator complex subunit alpha / REG-alpha / Activator of multicatalytic protease subunit 1 / Proteasome activator 28 subunit alpha / PA28alpha


Mass: 28717.973 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Psme1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P97371
#2: Protein
Proteasome activator complex subunit 2 / 11S regulator complex subunit beta / REG-beta / Activator of multicatalytic protease subunit 2 / ...11S regulator complex subunit beta / REG-beta / Activator of multicatalytic protease subunit 2 / Proteasome activator 28 subunit beta / PA28beta


Mass: 27094.283 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Psme2, Pa28b1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P97372
#3: Chemical ChemComp-PO4 / PHOSPHATE ION / Phosphate


Mass: 94.971 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: PO4
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 246 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.92 Å3/Da / Density % sol: 57.83 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.5 / Details: 0.2 M KH2PO4, 9 % PEG3350

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Apr 6, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.9→40 Å / Num. obs: 96305 / % possible obs: 96.4 % / Redundancy: 2.3 % / Rmerge(I) obs: 0.059 / Net I/σ(I): 12.1
Reflection shellResolution: 2.9→3 Å / Rmerge(I) obs: 0.532 / Mean I/σ(I) obs: 2.3 / % possible all: 92.8

-
Processing

Software
NameVersionClassification
REFMAC5.8.0158refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5MSJ
Resolution: 2.9→15 Å / Cor.coef. Fo:Fc: 0.931 / Cor.coef. Fo:Fc free: 0.913 / SU B: 41.043 / SU ML: 0.351 / Cross valid method: THROUGHOUT / ESU R Free: 0.416 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.27226 4784 5 %RANDOM
Rwork0.24307 ---
obs0.24453 90889 96.29 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 82.625 Å2
Baniso -1Baniso -2Baniso -3
1--0.11 Å20 Å23.76 Å2
2---4.44 Å2-0 Å2
3---2.31 Å2
Refinement stepCycle: 1 / Resolution: 2.9→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms23437 0 15 246 23698
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.01923892
X-RAY DIFFRACTIONr_bond_other_d0.0010.0223010
X-RAY DIFFRACTIONr_angle_refined_deg0.9261.98432329
X-RAY DIFFRACTIONr_angle_other_deg0.821353571
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.35652901
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.42225.0991110
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.039154418
X-RAY DIFFRACTIONr_dihedral_angle_4_deg11.86815132
X-RAY DIFFRACTIONr_chiral_restr0.0430.23691
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.02125961
X-RAY DIFFRACTIONr_gen_planes_other0.0010.024411
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.4126.86611688
X-RAY DIFFRACTIONr_mcbond_other0.4126.86611687
X-RAY DIFFRACTIONr_mcangle_it0.78110.2914561
X-RAY DIFFRACTIONr_mcangle_other0.78110.2914562
X-RAY DIFFRACTIONr_scbond_it0.2246.86812204
X-RAY DIFFRACTIONr_scbond_other0.2246.86112193
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other0.46410.29417751
X-RAY DIFFRACTIONr_long_range_B_refined2.00481.21926496
X-RAY DIFFRACTIONr_long_range_B_other1.98381.21226482
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.904→2.977 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.355 333 -
Rwork0.345 6328 -
obs--94.59 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
11.3209-0.0782-0.2030.69460.22190.81680.02260.20010.0371-0.2695-0.06840.0137-0.1975-0.1540.04580.2210.0304-0.01630.1252-0.03310.0176-49.155-9.1555131.9306
21.847-0.3181-0.26590.67260.06550.3248-0.0320.0551-0.0069-0.23760.0716-0.06170.0097-0.0265-0.03960.2237-0.02230.00290.1721-0.09540.0639-44.2704-30.3585137.5797
32.13470.2499-0.13430.3778-0.10220.6176-0.00030.0549-0.3408-0.06480.0016-0.15230.165-0.0061-0.00130.10480.00750.02090.0421-0.06030.1745-31.2263-38.0279154.2662
41.17260.6378-0.4060.8504-0.08660.3901-0.0245-0.0526-0.14790.07220.0353-0.20020.1010.0709-0.01070.05560.0237-0.06940.12180.03890.1816-21.5091-27.3743169.1315
50.92750.1952-0.6441.1366-0.1710.53010.1067-0.1184-0.01220.1726-0.0595-0.2365-0.11450.1007-0.04720.1115-0.05-0.05120.18570.00470.121-19.317-5.2156171.711
60.38540.1603-0.21450.4846-0.28521.75690.0041-0.05230.05420.0207-0.0492-0.1287-0.1358-0.0030.04510.2074-0.02470.01190.06950.01040.0662-28.35839.7141160.7336
70.47280.1424-0.07130.59090.08210.8597-0.00350.06410.1068-0.1501-0.0384-0.0159-0.1915-0.14080.04190.2230.0114-0.00080.05360.01880.0421-41.80758.803142.3236
81.25750.1067-1.43410.72850.03731.98840.06270.03490.07290.0681-0.07240.1566-0.2243-0.01640.00960.1883-0.03240.06390.0761-0.05510.1437-89.315712.597195.601
90.85950.8396-0.90321.3927-1.1171.80030.1058-0.07590.05140.2538-0.07150.0377-0.28990.0765-0.03440.1739-0.05620.06880.1025-0.08180.0767-78.1160.9002211.0708
102.76710.8348-0.92860.8817-0.33890.82490.1233-0.27420.00260.2456-0.08040.0124-0.11950.1273-0.04290.2106-0.03430.00560.11980.03220.0335-75.7743-21.1009213.4385
112.21-0.1039-0.62640.54740.04350.4470.03970.0157-0.11930.2131-0.02470.04620.05080.0302-0.0150.1686-0.01370.00650.04840.05980.1375-85.5489-36.6025201.4682
121.6462-0.3821-0.65951.04930.23810.85240.05520.0721-0.25920.0453-0.03690.17890.0845-0.0675-0.01830.1069-0.0595-0.02890.04230.00420.1239-99.1122-34.3594183.7415
130.879-0.6504-0.53941.22340.23270.46710.0460.1055-0.0161-0.08390.0140.1350.0468-0.035-0.060.05810.0173-0.07620.1617-0.01590.1828-105.3417-16.8611173.5192
140.99180.0389-0.83090.78460.29451.73840.06130.19080.1904-0.0640.04110.3065-0.2133-0.0056-0.10240.08040.0408-0.01320.11450.03690.2235-101.33394.8683178.8909
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A4 - 242
2X-RAY DIFFRACTION2B7 - 243
3X-RAY DIFFRACTION3C6 - 243
4X-RAY DIFFRACTION4D4 - 243
5X-RAY DIFFRACTION5E4 - 242
6X-RAY DIFFRACTION6F3 - 244
7X-RAY DIFFRACTION7G3 - 242
8X-RAY DIFFRACTION8H6 - 242
9X-RAY DIFFRACTION9I9 - 243
10X-RAY DIFFRACTION10J7 - 242
11X-RAY DIFFRACTION11K5 - 242
12X-RAY DIFFRACTION12L4 - 242
13X-RAY DIFFRACTION13M5 - 244
14X-RAY DIFFRACTION14N6 - 242

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more