[English] 日本語
Yorodumi
- PDB-2n3v: Solution structure of the Rpn1 T1 site with K48-linked diubiquiti... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2n3v
TitleSolution structure of the Rpn1 T1 site with K48-linked diubiquitin in the extended binding mode
Components
  • 26S proteasome regulatory subunit RPN1
  • Ubiquitin-60S ribosomal protein L40
KeywordsPROTEIN BINDING
Function / homology
Function and homology information


proteasome regulatory particle, base subcomplex / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Regulation of PTEN stability and activity / CDK-mediated phosphorylation and removal of Cdc6 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / KEAP1-NFE2L2 pathway / Neddylation / Orc1 removal from chromatin ...proteasome regulatory particle, base subcomplex / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Regulation of PTEN stability and activity / CDK-mediated phosphorylation and removal of Cdc6 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / KEAP1-NFE2L2 pathway / Neddylation / Orc1 removal from chromatin / MAPK6/MAPK4 signaling / regulation of protein catabolic process / proteasome storage granule / Peptide chain elongation / Antigen processing: Ubiquitination & Proteasome degradation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / Response of EIF2AK4 (GCN2) to amino acid deficiency / SRP-dependent cotranslational protein targeting to membrane / Viral mRNA Translation / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / GTP hydrolysis and joining of the 60S ribosomal subunit / Ub-specific processing proteases / L13a-mediated translational silencing of Ceruloplasmin expression / Major pathway of rRNA processing in the nucleolus and cytosol / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / enzyme regulator activity / Maturation of protein E / Maturation of protein E / cytosolic ribosome / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / Neutrophil degranulation / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Membrane binding and targetting of GAG proteins / Endosomal Sorting Complex Required For Transport (ESCRT) / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / Negative regulation of FLT3 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Constitutive Signaling by NOTCH1 HD Domain Mutants / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / Regulation of FZD by ubiquitination / Downregulation of ERBB4 signaling / p75NTR recruits signalling complexes / APC-Cdc20 mediated degradation of Nek2A / InlA-mediated entry of Listeria monocytogenes into host cells / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Regulation of pyruvate metabolism / Regulation of innate immune responses to cytosolic DNA / NF-kB is activated and signals survival / proteasome complex / Downregulation of ERBB2:ERBB3 signaling / Pexophagy / NRIF signals cell death from the nucleus / Regulation of PTEN localization / VLDLR internalisation and degradation / Activated NOTCH1 Transmits Signal to the Nucleus / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Regulation of BACH1 activity / MAP3K8 (TPL2)-dependent MAPK1/3 activation / TICAM1, RIP1-mediated IKK complex recruitment / Translesion synthesis by REV1 / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Translesion synthesis by POLK / InlB-mediated entry of Listeria monocytogenes into host cell / Downregulation of TGF-beta receptor signaling / Josephin domain DUBs / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Regulation of activated PAK-2p34 by proteasome mediated degradation / Translesion synthesis by POLI / IKK complex recruitment mediated by RIP1 / Gap-filling DNA repair synthesis and ligation in GG-NER / PINK1-PRKN Mediated Mitophagy / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / TNFR1-induced NF-kappa-B signaling pathway / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / TCF dependent signaling in response to WNT / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Regulation of NF-kappa B signaling / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / activated TAK1 mediates p38 MAPK activation / Negative regulators of DDX58/IFIH1 signaling / TNFR2 non-canonical NF-kB pathway
Similarity search - Function
26S proteasome regulatory complex, non-ATPase subcomplex, Rpn1 subunit / RPN1, N-terminal / 26S proteasome non-ATPase regulatory subunit RPN1, C-terminal / RPN1 N-terminal domain / 26S proteasome non-ATPase regulatory subunit RPN1 C-terminal / Proteasome/cyclosome repeat / Proteasome/cyclosome repeat / Ribosomal L40e family / Ribosomal_L40e / Ribosomal protein L40e ...26S proteasome regulatory complex, non-ATPase subcomplex, Rpn1 subunit / RPN1, N-terminal / 26S proteasome non-ATPase regulatory subunit RPN1, C-terminal / RPN1 N-terminal domain / 26S proteasome non-ATPase regulatory subunit RPN1 C-terminal / Proteasome/cyclosome repeat / Proteasome/cyclosome repeat / Ribosomal L40e family / Ribosomal_L40e / Ribosomal protein L40e / Ribosomal protein L40e superfamily / : / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Armadillo-like helical / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Armadillo-type fold / Ubiquitin-like domain superfamily
Similarity search - Domain/homology
26S proteasome regulatory subunit RPN1 / Ubiquitin-ribosomal protein eL40 fusion protein
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
Homo sapiens (human)
MethodSOLUTION NMR / simulated annealing
AuthorsChen, X. / Walters, K.J.
CitationJournal: Science / Year: 2016
Title: Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome.
Authors: Shi, Y. / Chen, X. / Elsasser, S. / Stocks, B.B. / Tian, G. / Lee, B.H. / Shi, Y. / Zhang, N. / de Poot, S.A. / Tuebing, F. / Sun, S. / Vannoy, J. / Tarasov, S.G. / Engen, J.R. / Finley, D. / Walters, K.J.
History
DepositionJun 10, 2015Deposition site: BMRB / Processing site: RCSB
Revision 1.0Feb 24, 2016Provider: repository / Type: Initial release
Revision 1.1Mar 23, 2016Group: Database references
Revision 1.2Jun 14, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_nmr_spectrometer / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_conn.pdbx_leaving_atom_flag
Revision 1.3Nov 6, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: 26S proteasome regulatory subunit RPN1
B: Ubiquitin-60S ribosomal protein L40
C: Ubiquitin-60S ribosomal protein L40


Theoretical massNumber of molelcules
Total (without water)30,7903
Polymers30,7903
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2380 Å2
ΔGint-10 kcal/mol
Surface area16140 Å2
MethodPISA
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 50
RepresentativeModel #1

-
Components

#1: Protein 26S proteasome regulatory subunit RPN1 / HMG-CoA reductase degradation protein 2 / Proteasome non-ATPase subunit 1


Mass: 13636.592 Da / Num. of mol.: 1 / Fragment: UNP residues 482-612
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: RPN1, HRD2, NAS1, RPD1, YHR027C / Plasmid: Pgex4t1 / Production host: Escherichia coli (E. coli) / References: UniProt: P38764
#2: Protein Ubiquitin-60S ribosomal protein L40 / CEP52 / Ubiquitin A-52 residue ribosomal protein fusion product 1 / Ubiquitin / 60S ribosomal protein L40


Mass: 8576.831 Da / Num. of mol.: 2 / Fragment: UNP residues 1-76
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBA52, UBCEP2 / Plasmid: Pet3a / Production host: Escherichia coli (E. coli) / References: UniProt: P62987
Has protein modificationY

-
Experimental details

-
Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
2212D 1H-13C HSQC aliphatic
3313D 1H-13C NOESY aliphatic
4413D 13C-HALF FILTER NOESY
5514D HMQC-NOESY-HMQC

-
Sample preparation

Details
Solution-IDContents
10.3 MM [U-100% 15N] PROTEIN_1, 0.04-1.2 MM PROTEIN_2, 50 MM HEPES, 50 MM SODIUM CHLORIDE, 1 MM EDTA, 2 MM DTT, 0.1 % SODIUM AZIDE, 95% H2O/5% D2O
20.08-0.3 MM PROTEIN_1, 0.3 MM [U-100% 15N] PROTEIN_2, 50 MM HEPES, 50 MM SODIUM CHLORIDE, 1 MM EDTA, 2 MM DTT, 0.1 % SODIUM AZIDE, 95% H2O/ 5% D2O
30.06-0.5 MM PROTEIN_1, 0.5 MM [U-13C] PROTEIN_2, 50 MM HEPES, 50 MM SODIUM CHLORIDE, 1 MM EDTA, 2 MM DTT, 0.1 % SODIUM AZIDE, 100% D2O
40.6 MM [U-13C] PROTEIN_1, 0.6 MM PROTEIN_2, 50 MM HEPES, 50 MM SODIUM CHLORIDE, 1 MM EDTA, 2 MM DTT, 0.1 % SODIUM AZIDE, 100% D2O
50.5 MM PROTEIN_ 1, 0.5 MM [U-13C] PROTEIN_2, 50 MM HEPES, 50 MM SODIUM CHLORIDE, 1 MM EDTA, 2 MM DTT, 0.1 % SODIUM AZIDE, 100% D2O
60.6 MM [U-13C] PROTEIN_1, 0.12-0.6 MM PROTEIN_2, 50 MM HEPES, 50 MM SODIUM CHLORIDE, 1 MM EDTA, 2 MM DTT, 0.1 % SODIUM AZIDE, 100% D2O
Sample
Conc. (mg/ml)UnitsComponentIsotopic labelingConc. range (mg/ml)Solution-ID
0.3 mMentity_1-1[U-100% 15N]1
mMentity_2-20.04-1.21
50 mMHEPES-31
50 mMsodium chloride-41
1 mMEDTA-51
2 mMDTT-61
0.1 %sodium azide-71
mMentity_1-80.08-0.32
0.3 mMentity_2-9[U-100% 15N]2
50 mMHEPES-102
50 mMsodium chloride-112
1 mMEDTA-122
2 mMDTT-132
0.1 %sodium azide-142
mMentity_1-150.06-0.53
0.5 mMentity_2-16[U-13C]3
50 mMHEPES-173
50 mMsodium chloride-183
1 mMEDTA-193
2 mMDTT-203
0.1 %sodium azide-213
0.6 mMentity_1-22[U-13C]4
0.6 mMentity_2-234
50 mMHEPES-244
50 mMsodium chloride-254
1 mMEDTA-264
2 mMDTT-274
0.1 %sodium azide-284
0.5 mMentity_1-295
0.5 mMentity_2-30[U-13C]5
50 mMHEPES-315
50 mMsodium chloride-325
1 mMEDTA-335
2 mMDTT-345
0.1 %sodium azide-355
0.6 mMentity_1-36[U-13C]6
mMentity_2-370.12-0.66
50 mMHEPES-386
50 mMsodium chloride-396
1 mMEDTA-406
2 mMDTT-416
0.1 %sodium azide-426
Sample conditionsIonic strength: 50 / pH: 6.7 / Pressure: AMBIENT / Temperature: 298 K

-
NMR measurement

NMR spectrometerType: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 850 MHz

-
Processing

NMR software
NameVersionDeveloperClassification
X-PLOR NIHSCHWIETERS, KUSZEWSKI, TJrefinement
TopSpinstructure solution
NMRPipestructure solution
XEASYstructure solution
X-PLOR NIHNIHstructure solution
TALOSstructure solution
PROCHECKNMRstructure solution
RefinementMethod: simulated annealing / Software ordinal: 1
NMR ensembleConformers calculated total number: 50 / Conformers submitted total number: 10

+
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