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Entry
Database: EMDB / ID: EMD-8678
TitleConformational Landscape of the p28-Bound Human Proteasome Regulatory Particle
Map dataFinal Map of Rpn1-p28-AAA subcomplex in the TA2 state, corrected with a B-factor of -400
Sample
  • Complex: Proteasome regulatory particle
    • Protein or peptide: 26S proteasome non-ATPase regulatory subunit 10
    • Protein or peptide: 26S proteasome regulatory subunit 7
    • Protein or peptide: 26S proteasome regulatory subunit 4
    • Protein or peptide: 26S proteasome regulatory subunit 6B
    • Protein or peptide: 26S proteasome regulatory subunit 10B
    • Protein or peptide: 26S proteasome regulatory subunit 6A
    • Protein or peptide: 26S proteasome regulatory subunit 8
    • Protein or peptide: 26S proteasome non-ATPase regulatory subunit 2
Keywordsp28 / 26S proteasome / regulatory particle / 19S / gankyrin / HYDROLASE
Function / homology
Function and homology information


: / proteasome regulatory particle assembly / positive regulation of inclusion body assembly / thyrotropin-releasing hormone receptor binding / modulation by host of viral transcription / proteasome accessory complex / proteasome regulatory particle / cytosolic proteasome complex / positive regulation of proteasomal protein catabolic process / proteasome-activating activity ...: / proteasome regulatory particle assembly / positive regulation of inclusion body assembly / thyrotropin-releasing hormone receptor binding / modulation by host of viral transcription / proteasome accessory complex / proteasome regulatory particle / cytosolic proteasome complex / positive regulation of proteasomal protein catabolic process / proteasome-activating activity / proteasome regulatory particle, base subcomplex / negative regulation of programmed cell death / intermediate filament cytoskeleton / Regulation of ornithine decarboxylase (ODC) / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis / transcription factor binding / regulation of protein catabolic process / negative regulation of release of cytochrome c from mitochondria / proteasome storage granule / negative regulation of DNA damage response, signal transduction by p53 class mediator / negative regulation of NF-kappaB transcription factor activity / blastocyst development / general transcription initiation factor binding / positive regulation of RNA polymerase II transcription preinitiation complex assembly / negative regulation of MAPK cascade / positive regulation of cyclin-dependent protein serine/threonine kinase activity / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / enzyme regulator activity / ERAD pathway / cytoskeletal protein binding / inclusion body / proteasome complex / Regulation of activated PAK-2p34 by proteasome mediated degradation / protein localization to plasma membrane / positive regulation of protein ubiquitination / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / TNFR2 non-canonical NF-kB pathway / AUF1 (hnRNP D0) binds and destabilizes mRNA / Vpu mediated degradation of CD4 / Assembly of the pre-replicative complex / Degradation of DVL / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Dectin-1 mediated noncanonical NF-kB signaling / Degradation of AXIN / Hh mutants are degraded by ERAD / Activation of NF-kappaB in B cells / Degradation of GLI1 by the proteasome / P-body / Hedgehog ligand biogenesis / G2/M Checkpoints / Defective CFTR causes cystic fibrosis / Negative regulation of NOTCH4 signaling / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Autodegradation of the E3 ubiquitin ligase COP1 / Vif-mediated degradation of APOBEC3G / Regulation of RUNX3 expression and activity / Hedgehog 'on' state / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome / MAPK6/MAPK4 signaling / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / Degradation of beta-catenin by the destruction complex / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / ABC-family proteins mediated transport / CDK-mediated phosphorylation and removal of Cdc6 / SCF(Skp2)-mediated degradation of p27/p21 / CLEC7A (Dectin-1) signaling / Regulation of expression of SLITs and ROBOs / FCERI mediated NF-kB activation / Regulation of PTEN stability and activity / cytoplasmic ribonucleoprotein granule / Interleukin-1 signaling / Orc1 removal from chromatin / Regulation of RAS by GAPs / osteoblast differentiation / Separation of Sister Chromatids / Regulation of RUNX2 expression and activity / The role of GTSE1 in G2/M progression after G2 checkpoint / UCH proteinases / KEAP1-NFE2L2 pathway / Antigen processing: Ubiquitination & Proteasome degradation / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Downstream TCR signaling / Neddylation / RUNX1 regulates transcription of genes involved in differentiation of HSCs / ER-Phagosome pathway / protein-macromolecule adaptor activity / ubiquitin-dependent protein catabolic process / positive regulation of cell growth / cytoplasmic vesicle / secretory granule lumen
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 / : / 26S proteasome regulatory subunit 7, OB domain / Proteasome/cyclosome repeat / Proteasome/cyclosome repeat ...: / 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 / : / 26S proteasome regulatory subunit 7, OB domain / Proteasome/cyclosome repeat / Proteasome/cyclosome repeat / : / Proteasomal ATPase OB C-terminal domain / Proteasomal ATPase OB C-terminal domain / AAA ATPase, AAA+ lid domain / AAA+ lid domain / ATPase, AAA-type, conserved site / AAA-protein family signature. / Ankyrin repeat / Ankyrin repeats (3 copies) / ATPase family associated with various cellular activities (AAA) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / ATPase, AAA-type, core / Ankyrin repeat-containing domain superfamily / Armadillo-like helical / Armadillo-type fold / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Nucleic acid-binding, OB-fold / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
26S proteasome non-ATPase regulatory subunit 10 / 26S proteasome regulatory subunit 6A / 26S proteasome regulatory subunit 7 / 26S proteasome regulatory subunit 6B / 26S proteasome regulatory subunit 4 / 26S proteasome regulatory subunit 8 / 26S proteasome regulatory subunit 10B / 26S proteasome non-ATPase regulatory subunit 2
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 8.3 Å
AuthorsLu Y / Wu J
CitationJournal: Mol Cell / Year: 2017
Title: Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle.
Authors: Ying Lu / Jiayi Wu / Yuanchen Dong / Shuobing Chen / Shuangwu Sun / Yong-Bei Ma / Qi Ouyang / Daniel Finley / Marc W Kirschner / Youdong Mao /
Abstract: The proteasome holoenzyme is activated by its regulatory particle (RP) consisting of two subcomplexes, the lid and the base. A key event in base assembly is the formation of a heterohexameric ring of ...The proteasome holoenzyme is activated by its regulatory particle (RP) consisting of two subcomplexes, the lid and the base. A key event in base assembly is the formation of a heterohexameric ring of AAA-ATPases, which is guided by at least four RP assembly chaperones in mammals: PAAF1, p28/gankyrin, p27/PSMD9, and S5b. Using cryogenic electron microscopy, we analyzed the non-AAA structure of the p28-bound human RP at 4.5 Å resolution and determined seven distinct conformations of the Rpn1-p28-AAA subcomplex within the p28-bound RP at subnanometer resolutions. Remarkably, the p28-bound AAA ring does not form a channel in the free RP and spontaneously samples multiple "open" and "closed" topologies at the Rpt2-Rpt6 and Rpt3-Rpt4 interfaces. Our analysis suggests that p28 assists the proteolytic core particle to select a specific conformation of the ATPase ring for RP engagement and is released in a shoehorn-like fashion in the last step of the chaperone-mediated proteasome assembly.
History
DepositionApr 13, 2017-
Header (metadata) releaseAug 23, 2017-
Map releaseAug 23, 2017-
UpdateMar 13, 2024-
Current statusMar 13, 2024Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.003
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  • Surface level: 0.003
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  • Atomic models: PDB-5vhm
  • Surface level: 0.003
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_8678.png

Downloads & links

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Map

FileDownload / File: emd_8678.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationFinal Map of Rpn1-p28-AAA subcomplex in the TA2 state, corrected with a B-factor of -400
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.86 Å/pix.
x 360 pix.
= 309.6 Å		0.86 Å/pix.
x 360 pix.
= 309.6 Å		0.86 Å/pix.
x 360 pix.
= 309.6 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.86 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.003 / Movie #1: 0.003
Minimum - Maximum-0.0054027215 - 0.008979565
Average (Standard dev.)-0.00014249163 (±0.0006886866)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 309.6 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z0.860.860.86
M x/y/z360360360
origin x/y/z0.0000.0000.000
length x/y/z309.600309.600309.600
α/β/γ90.00090.00090.000
start NX/NY/NZ-69-50-137
NX/NY/NZ136114193
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS360360360
D min/max/mean-0.0050.009-0.000

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Supplemental data

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Sample components

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Entire : Proteasome regulatory particle

EntireName: Proteasome regulatory particle
Components
  • Complex: Proteasome regulatory particle
    • Protein or peptide: 26S proteasome non-ATPase regulatory subunit 10
    • Protein or peptide: 26S proteasome regulatory subunit 7
    • Protein or peptide: 26S proteasome regulatory subunit 4
    • Protein or peptide: 26S proteasome regulatory subunit 6B
    • Protein or peptide: 26S proteasome regulatory subunit 10B
    • Protein or peptide: 26S proteasome regulatory subunit 6A
    • Protein or peptide: 26S proteasome regulatory subunit 8
    • Protein or peptide: 26S proteasome non-ATPase regulatory subunit 2

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Supramolecule #1: Proteasome regulatory particle

SupramoleculeName: Proteasome regulatory particle / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: 26S proteasome non-ATPase regulatory subunit 10

MacromoleculeName: 26S proteasome non-ATPase regulatory subunit 10 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 24.14249 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: CVSNLMVCNL AYSGKLEELK ESILADKSLA TRTDQDSRTA LHWACSAGHT EIVEFLLQLG VPVNDKDDAG WSPLHIAASA GRDEIVKAL LGKGAQVNAV NQNGCTPLHY AASKNRHEIA VMLLEGGANP DAKDHYEATA MHRAAAKGNL KMIHILLYYK A STNIQDTE ...String:
CVSNLMVCNL AYSGKLEELK ESILADKSLA TRTDQDSRTA LHWACSAGHT EIVEFLLQLG VPVNDKDDAG WSPLHIAASA GRDEIVKAL LGKGAQVNAV NQNGCTPLHY AASKNRHEIA VMLLEGGANP DAKDHYEATA MHRAAAKGNL KMIHILLYYK A STNIQDTE GNTPLHLACD EERVEEAKLL VSQGASIYIE NKEEKTPLQV AKGGLGLILK RMVEG

UniProtKB: 26S proteasome non-ATPase regulatory subunit 10

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Macromolecule #2: 26S proteasome regulatory subunit 7

MacromoleculeName: 26S proteasome regulatory subunit 7 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.746465 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: PTVTMMQVEE KPDVTYSDVG GCKEQIEKLR EVVETPLLHP ERFVNLGIEP PKGVLLFGPP GTGKTLCARA VANRTDACFI RVIGSELVQ KYVGEGARMV RELFEMARTK KACLIFFDEI DAIGGARFDD GAGGDNEVQR TMLELINQLD GFDPRGNIKV L MATNRPDT ...String:
PTVTMMQVEE KPDVTYSDVG GCKEQIEKLR EVVETPLLHP ERFVNLGIEP PKGVLLFGPP GTGKTLCARA VANRTDACFI RVIGSELVQ KYVGEGARMV RELFEMARTK KACLIFFDEI DAIGGARFDD GAGGDNEVQR TMLELINQLD GFDPRGNIKV L MATNRPDT LDPALMRPGR LDRKIEFSLP DLEGRTHIFK IHARSMSVER DIRFELLARL CPNSTGAEIR SVCTEAGMFA IR ARRKIAT EKDFLEAVNK VIKSYAKFS

UniProtKB: 26S proteasome regulatory subunit 7

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Macromolecule #3: 26S proteasome regulatory subunit 4

MacromoleculeName: 26S proteasome regulatory subunit 4 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.901344 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: TDPLVTVMKV EKAPQETYAD IGGLDNQIQE IKESVELPLT HPEYYEEMGI KPPKGVILYG PPGTGKTLLA KAVANQTSAT FLRVVGSEL IQKYLGDGPK LVRELFRVAE EHAPSIVFID EIDAIGTKRY DSNSGGEREI QRTMLELLNQ LDGFDSRGDV K VIMATNRI ...String:
TDPLVTVMKV EKAPQETYAD IGGLDNQIQE IKESVELPLT HPEYYEEMGI KPPKGVILYG PPGTGKTLLA KAVANQTSAT FLRVVGSEL IQKYLGDGPK LVRELFRVAE EHAPSIVFID EIDAIGTKRY DSNSGGEREI QRTMLELLNQ LDGFDSRGDV K VIMATNRI ETLDPALIRP GRIDRKIEFP LPDEKTKKRI FQIHTSRMTL ADDVTLDDLI MAKDDLSGAD IKAICTEAGL MA LRERRMK VTNEDFKKSK ENVLYKKQE

UniProtKB: 26S proteasome regulatory subunit 4

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Macromolecule #4: 26S proteasome regulatory subunit 6B

MacromoleculeName: 26S proteasome regulatory subunit 6B / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.497975 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: PEADSSIMML TSDQKPDVMY ADIGGMDIQK QEVREAVELP LTHFELYKQI GIDPPRGVLM YGPPGCGKTM LAKAVAHHTT AAFIRVVGS EFVQKYLGEG PRMVRDVFRL AKENAPAIIF IDEIDAIATK RFDAQTGADR EVQRILLELL NQMDGFDQNV N VKVIMATN ...String:
PEADSSIMML TSDQKPDVMY ADIGGMDIQK QEVREAVELP LTHFELYKQI GIDPPRGVLM YGPPGCGKTM LAKAVAHHTT AAFIRVVGS EFVQKYLGEG PRMVRDVFRL AKENAPAIIF IDEIDAIATK RFDAQTGADR EVQRILLELL NQMDGFDQNV N VKVIMATN RADTLDPALL RPGRLDRKIE FPLPDRRQKR LIFSTITSKM NLSEEVDLED YVARPDKISG ADINSICQES GM LAVRENR YIVLAKDFEK AYKTV

UniProtKB: 26S proteasome regulatory subunit 6B

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Macromolecule #5: 26S proteasome regulatory subunit 10B

MacromoleculeName: 26S proteasome regulatory subunit 10B / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.434889 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: GNVSYSEIGG LSEQIRELRE VIELPLTNPE LFQRVGIIPP KGCLLYGPPG TGKTLLARAV ASQLDCNFLK VVSSSIVDKY IGESARLIR EMFNYARDHQ PCIIFMDEID AIGGRRFSEG TSADREIQRT LMELLNQMDG FDTLHRVKMI MATNRPDTLD P ALLRPGRL ...String:
GNVSYSEIGG LSEQIRELRE VIELPLTNPE LFQRVGIIPP KGCLLYGPPG TGKTLLARAV ASQLDCNFLK VVSSSIVDKY IGESARLIR EMFNYARDHQ PCIIFMDEID AIGGRRFSEG TSADREIQRT LMELLNQMDG FDTLHRVKMI MATNRPDTLD P ALLRPGRL DRKIHIDLPN EQARLDILKI HAGPITKHGE IDYEAIVKLS DGFNGADLRN VCTEAGMFAI RADHDFVVQE DF MKAVRKV ADSKKLESKL DYKPV

UniProtKB: 26S proteasome regulatory subunit 10B

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Macromolecule #6: 26S proteasome regulatory subunit 6A

MacromoleculeName: 26S proteasome regulatory subunit 6A / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.773246 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: TEYDSRVKAM EVDERPTEQY SDIGGLDKQI QELVEAIVLP MNHKEKFENL GIQPPKGVLM YGPPGTGKTL LARACAAQTK ATFLKLAGP QLVQMFIGDG AKLVRDAFAL AKEKAPSIIF IDELDAIGTK RFDSEKAGDR EVQRTMLELL NQLDGFQPNT Q VKVIAATN ...String:
TEYDSRVKAM EVDERPTEQY SDIGGLDKQI QELVEAIVLP MNHKEKFENL GIQPPKGVLM YGPPGTGKTL LARACAAQTK ATFLKLAGP QLVQMFIGDG AKLVRDAFAL AKEKAPSIIF IDELDAIGTK RFDSEKAGDR EVQRTMLELL NQLDGFQPNT Q VKVIAATN RVDILDPALL RSGRLDRKIE FPMPNEEARA RIMQIHSRKM NVSPDVNYEE LARCTDDFNG AQCKAVCVEA GM IALRRGA TELTHEDYME GILEVQAKKK

UniProtKB: 26S proteasome regulatory subunit 6A

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Macromolecule #7: 26S proteasome regulatory subunit 8

MacromoleculeName: 26S proteasome regulatory subunit 8 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.501363 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: KVDPLVSLMM VEKVPDSTYE MIGGLDKQIK EIKEVIELPV KHPELFEALG IAQPKGVLLY GPPGTGKTLL ARAVAHHTDC TFIRVSGSE LVQKFIGEGA RMVRELFVMA REHAPSIIFM DEIDSIGSSR LEGGSGGDSE VQRTMLELLN QLDGFEATKN I KVIMATNR ...String:
KVDPLVSLMM VEKVPDSTYE MIGGLDKQIK EIKEVIELPV KHPELFEALG IAQPKGVLLY GPPGTGKTLL ARAVAHHTDC TFIRVSGSE LVQKFIGEGA RMVRELFVMA REHAPSIIFM DEIDSIGSSR LEGGSGGDSE VQRTMLELLN QLDGFEATKN I KVIMATNR IDILDSALLR PGRIDRKIEF PPPNEEARLD ILKIHSRKMN LTRGINLRKI AELMPGASGA EVKGVCTEAG MY ALRERRV HVTQEDFEMA VAKVMQKDS

UniProtKB: 26S proteasome regulatory subunit 8

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Macromolecule #8: 26S proteasome non-ATPase regulatory subunit 2

MacromoleculeName: 26S proteasome non-ATPase regulatory subunit 2 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 93.790188 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: RDKAPVQPQQ SPAAAPGGTD EKPSGKERRD AGDKDKEQEL SEEDKQLQDE LEMLVERLGE KDTSLYRPAL EELRRQIRSS TTSMTSVPK PLKFLRPHYG KLKEIYENMA PGENKRFAAD IISVLAMTMS GERECLKYRL VGSQEELASW GHEYVRHLAG E VAKEWQEL ...String:
RDKAPVQPQQ SPAAAPGGTD EKPSGKERRD AGDKDKEQEL SEEDKQLQDE LEMLVERLGE KDTSLYRPAL EELRRQIRSS TTSMTSVPK PLKFLRPHYG KLKEIYENMA PGENKRFAAD IISVLAMTMS GERECLKYRL VGSQEELASW GHEYVRHLAG E VAKEWQEL DDAEKVQREP LLTLVKEIVP YNMAHNAEHE ACDLLMEIEQ VDMLEKDIDE NAYAKVCLYL TSCVNYVPEP EN SALLRCA LGVFRKFSRF PEALRLALML NDMELVEDIF TSCKDVVVQK QMAFMLGRHG VFLELSEDVE EYEDLTEIMS NVQ LNSNFL ALARELDIME PKVPDDIYKT HLENNRFGGS GSQVDSARMN LASSFVNGFV NAAFGQDKLL TDDGNKWLYK NKDH GMLSA AASLGMILLW DVDGGLTQID KYLYSSEDYI KSGALLACGI VNSGVRNECD PALALLSDYV LHNSNTMRLG SIFGL GLAY AGSNREDVLT LLLPVMGDSK SSMEVAGVTA LACGMIAVGS CNGDVTSTIL QTIMEKSETE LKDTYARWLP LGLGLN HLG KGEAIEAILA ALEVVSEPFR SFANTLVDVC AYAGSGNVLK VQQLLHICSE HFDSKEKEED KDKKEKKDKD KKEAPAD MG AHQGVAVLGI ALIAMGEEIG AEMALRTFGH LLRYGEPTLR RAVPLALALI SVSNPRLNIL DTLSKFSHDA DPEVSYNS I FAMGMVGSGT NNARLAAMLR QLAQYHAKDP NNLFMVRLAQ GLTHLGKGTL TLCPYHSDRQ LMSQVAVAGL LTVLVSFLD VRNIILGKSH YVLYGLVAAM QPRMLVTFDE ELRPLPVSVR VGQAVDVV

UniProtKB: 26S proteasome non-ATPase regulatory subunit 2

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TECNAI ARCTICA
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company

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Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 8.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 11082
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: PROJECTION MATCHING

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