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- EMDB-18761: Human preholo proteasome 20S core particle -

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Basic information

Entry
Database: EMDB / ID: EMD-18761
TitleHuman preholo proteasome 20S core particle
Map data
Sample
  • Complex: Human preholo proteasome 20S core particle
    • Protein or peptide: x 17 types
KeywordsComplex / HYDROLASE
Function / homology
Function and homology information


purine ribonucleoside triphosphate binding / CD8-positive, alpha-beta T cell differentiation / thymic T cell selection / CD8-positive, alpha-beta T cell homeostasis / Antigen processing: Ub, ATP-independent proteasomal degradation / proteasome core complex assembly / T-helper 1 cell differentiation / negative regulation of regulatory T cell differentiation / cellular response to type I interferon / Regulation of ornithine decarboxylase (ODC) ...purine ribonucleoside triphosphate binding / CD8-positive, alpha-beta T cell differentiation / thymic T cell selection / CD8-positive, alpha-beta T cell homeostasis / Antigen processing: Ub, ATP-independent proteasomal degradation / proteasome core complex assembly / T-helper 1 cell differentiation / negative regulation of regulatory T cell differentiation / cellular response to type I interferon / Regulation of ornithine decarboxylase (ODC) / proteasome core complex / Proteasome assembly / T-helper 17 cell differentiation / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis / flagellated sperm motility / proteasome binding / myofibril / AMPK-induced ERAD and lysosome mediated degradation of PD-L1(CD274) / GSK3B-mediated proteasomal degradation of PD-L1(CD274) / SPOP-mediated proteasomal degradation of PD-L1(CD274) / proteasomal ubiquitin-independent protein catabolic process / protein folding chaperone complex / Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide / proteasome storage granule / proteasome endopeptidase complex / chaperone-mediated protein complex assembly / NF-kappaB binding / proteasome core complex, beta-subunit complex / threonine-type endopeptidase activity / proteasome core complex, alpha-subunit complex / proteasome assembly / immune system process / regulation of G1/S transition of mitotic cell cycle / ciliary tip / response to type II interferon / positive regulation of interleukin-2 production / regulation of proteasomal protein catabolic process / : / proteasome complex / sarcomere / proteasomal protein catabolic process / Regulation of activated PAK-2p34 by proteasome mediated degradation / sperm end piece / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / negative regulation of inflammatory response to antigenic stimulus / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / lipopolysaccharide binding / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / AUF1 (hnRNP D0) binds and destabilizes mRNA / TNFR2 non-canonical NF-kB pathway / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / P-body / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Dectin-1 mediated noncanonical NF-kB signaling / Degradation of DVL / Degradation of AXIN / Degradation of CRY and PER proteins / meiotic cell cycle / Hh mutants are degraded by ERAD / Activation of NF-kappaB in B cells / G2/M Checkpoints / Degradation of GLI1 by the proteasome / Hedgehog ligand biogenesis / Regulation of RUNX3 expression and activity / Autodegradation of the E3 ubiquitin ligase COP1 / Defective CFTR causes cystic fibrosis / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Negative regulation of NOTCH4 signaling / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / Hedgehog 'on' state / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / Vif-mediated degradation of APOBEC3G / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / MAPK6/MAPK4 signaling / Degradation of CDH1 / Degradation of beta-catenin by the destruction complex / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / CDK-mediated phosphorylation and removal of Cdc6 / ABC-family protein mediated transport / CLEC7A (Dectin-1) signaling / response to virus / SCF(Skp2)-mediated degradation of p27/p21 / FCERI mediated NF-kB activation / nuclear matrix / Regulation of expression of SLITs and ROBOs / Regulation of PTEN stability and activity / Interleukin-1 signaling / positive regulation of type II interferon production / Orc1 removal from chromatin / Regulation of RUNX2 expression and activity / Regulation of RAS by GAPs / The role of GTSE1 in G2/M progression after G2 checkpoint / positive regulation of tumor necrosis factor production
Similarity search - Function
Proteasome assembly chaperone 1 / Proteasome assembly chaperone 4 / Proteasome assembly chaperone 2, eukaryotic / Proteasome maturation factor Ump1 / Proteasome maturation factor UMP1 / Proteasome assembly chaperone 2 / Proteasome assembly chaperone 2 superfamily / PAC2 family / Proteasome subunit alpha 1 / Proteasome beta subunit, C-terminal ...Proteasome assembly chaperone 1 / Proteasome assembly chaperone 4 / Proteasome assembly chaperone 2, eukaryotic / Proteasome maturation factor Ump1 / Proteasome maturation factor UMP1 / Proteasome assembly chaperone 2 / Proteasome assembly chaperone 2 superfamily / PAC2 family / Proteasome subunit alpha 1 / Proteasome beta subunit, C-terminal / Proteasome beta subunits C terminal / Proteasome subunit beta 4 / Proteasome subunit beta 2 / Proteasome beta 3 subunit / Proteasome subunit alpha5 / Proteasome subunit alpha6 / Proteasome beta-type subunits signature. / Peptidase T1A, proteasome beta-subunit / Proteasome beta-type subunit, conserved site / Proteasome subunit A N-terminal signature / Proteasome alpha-type subunits signature. / Proteasome alpha-subunit, N-terminal domain / Proteasome subunit A N-terminal signature Add an annotation / Proteasome B-type subunit / Proteasome beta-type subunit profile. / : / Proteasome alpha-type subunit / Proteasome alpha-type subunit profile. / Proteasome subunit / Proteasome, subunit alpha/beta / Nucleophile aminohydrolases, N-terminal
Similarity search - Domain/homology
Proteasome subunit alpha type-7 / Proteasome assembly chaperone 1 / Proteasome subunit beta type-1 / Proteasome subunit alpha type-1 / Proteasome subunit alpha type-2 / Proteasome subunit alpha type-3 / Proteasome subunit alpha type-4 / Proteasome subunit alpha type-5 / Proteasome subunit beta type-4 / Proteasome subunit beta type-6 ...Proteasome subunit alpha type-7 / Proteasome assembly chaperone 1 / Proteasome subunit beta type-1 / Proteasome subunit alpha type-1 / Proteasome subunit alpha type-2 / Proteasome subunit alpha type-3 / Proteasome subunit alpha type-4 / Proteasome subunit alpha type-5 / Proteasome subunit beta type-4 / Proteasome subunit beta type-6 / Proteasome subunit beta type-5 / Proteasome subunit beta type-3 / Proteasome subunit beta type-2 / Proteasome subunit alpha type-6 / Proteasome assembly chaperone 2 / Proteasome subunit beta type-7 / Proteasome maturation protein
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.89 Å
AuthorsSchulman BA / Hanna JW / Harper JW / Adolf F / Du J / Rawson SD / Walsh Jr RM / Goodall EA
Funding support Germany, United States, 4 items
OrganizationGrant numberCountry
Max Planck Society Germany
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) United States
National Institutes of Health/National Institute on Aging (NIH/NIA) United States
Aligning Science Across Parkinsons (ASAP)
CitationJournal: bioRxiv / Year: 2024
Title: Visualizing chaperone-mediated multistep assembly of the human 20S proteasome.
Authors: Frank Adolf / Jiale Du / Ellen A Goodall / Richard M Walsh / Shaun Rawson / Susanne von Gronau / J Wade Harper / John Hanna / Brenda A Schulman /
Abstract: Dedicated assembly factors orchestrate stepwise production of many molecular machines, including the 28-subunit proteasome core particle (CP) that mediates protein degradation. Here, we report cryo- ...Dedicated assembly factors orchestrate stepwise production of many molecular machines, including the 28-subunit proteasome core particle (CP) that mediates protein degradation. Here, we report cryo-EM reconstructions of seven recombinant human subcomplexes that visualize all five chaperones and the three active site propeptides across a wide swath of the assembly pathway. Comparison of these chaperone-bound intermediates and a matching mature CP reveals molecular mechanisms determining the order of successive subunit additions, and how proteasome subcomplexes and assembly factors structurally adapt upon progressive subunit incorporation to stabilize intermediates, facilitate the formation of subsequent intermediates, and ultimately rearrange to coordinate proteolytic activation with gated access to active sites. The structural findings reported here explain many previous biochemical and genetic observations. This work establishes a methodologic approach for structural analysis of multiprotein complex assembly intermediates, illuminates specific functions of assembly factors, and reveals conceptual principles underlying human proteasome biogenesis.
History
DepositionOct 26, 2023-
Header (metadata) releaseFeb 21, 2024-
Map releaseFeb 21, 2024-
UpdateJul 2, 2025-
Current statusJul 2, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_18761.png

Downloads & links

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Map

FileDownload / File: emd_18761.map.gz / Format: CCP4 / Size: 18.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
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Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.89 Å/pix.
x 168 pix.
= 316.68 Å		1.89 Å/pix.
x 168 pix.
= 316.68 Å		1.89 Å/pix.
x 168 pix.
= 316.68 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.885 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.37
Minimum - Maximum-1.3023485 - 2.688272
Average (Standard dev.)0.009443309 (±0.13885637)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions168168168
Spacing168168168
CellA=B=C: 316.68 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_18761_msk_1.map
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Additional map: #1

Fileemd_18761_additional_1.map
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Half map: #2

Fileemd_18761_half_map_1.map
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Half map: #1

Fileemd_18761_half_map_2.map
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Sample components

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Entire : Human preholo proteasome 20S core particle

EntireName: Human preholo proteasome 20S core particle
Components
  • Complex: Human preholo proteasome 20S core particle
    • Protein or peptide: Proteasome subunit alpha type-2
    • Protein or peptide: Proteasome subunit alpha type-4
    • Protein or peptide: Proteasome subunit alpha type-7
    • Protein or peptide: Proteasome subunit alpha type-5
    • Protein or peptide: Proteasome subunit alpha type-1
    • Protein or peptide: Proteasome subunit alpha type-3
    • Protein or peptide: Proteasome subunit alpha type-6
    • Protein or peptide: Proteasome maturation protein
    • Protein or peptide: Proteasome assembly chaperone 1
    • Protein or peptide: Proteasome assembly chaperone 2
    • Protein or peptide: Proteasome subunit beta type-7
    • Protein or peptide: Proteasome subunit beta type-3
    • Protein or peptide: Proteasome subunit beta type-2
    • Protein or peptide: Proteasome subunit beta type-5
    • Protein or peptide: Proteasome subunit beta type-1
    • Protein or peptide: Proteasome subunit beta type-4
    • Protein or peptide: Proteasome subunit beta type-6

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Supramolecule #1: Human preholo proteasome 20S core particle

SupramoleculeName: Human preholo proteasome 20S core particle / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Proteasome subunit alpha type-2

MacromoleculeName: Proteasome subunit alpha type-2 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 25.927535 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MAERGYSFSL TTFSPSGKLV QIEYALAAVA GGAPSVGIKA ANGVVLATEK KQKSILYDER SVHKVEPITK HIGLVYSGMG PDYRVLVHR ARKLAQQYYL VYQEPIPTAQ LVQRVASVMQ EYTQSGGVRP FGVSLLICGW NEGRPYLFQS DPSGAYFAWK A TAMGKNYV ...String:
MAERGYSFSL TTFSPSGKLV QIEYALAAVA GGAPSVGIKA ANGVVLATEK KQKSILYDER SVHKVEPITK HIGLVYSGMG PDYRVLVHR ARKLAQQYYL VYQEPIPTAQ LVQRVASVMQ EYTQSGGVRP FGVSLLICGW NEGRPYLFQS DPSGAYFAWK A TAMGKNYV NGKTFLEKRY NEDLELEDAI HTAILTLKES FEGQMTEDNI EVGICNEAGF RRLTPTEVKD YLAAIA

UniProtKB: Proteasome subunit alpha type-2

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Macromolecule #2: Proteasome subunit alpha type-4

MacromoleculeName: Proteasome subunit alpha type-4 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 27.901932 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: RRYDSRTTIF SPEGRLYQVE YAMEAIGHAG TCLGILANDG VLLAAERRNI HKLLDEVFFS EKIYKLNEDM ACSVAGITSD ANVLTNELR LIAQRYLLQY QEPIPCEQLV TALCDIKQAY TQFGGKRPFG VSLLYIGWDK HYGFQLYQSD PSGNYGGWKA T CIGNNSAA ...String:
RRYDSRTTIF SPEGRLYQVE YAMEAIGHAG TCLGILANDG VLLAAERRNI HKLLDEVFFS EKIYKLNEDM ACSVAGITSD ANVLTNELR LIAQRYLLQY QEPIPCEQLV TALCDIKQAY TQFGGKRPFG VSLLYIGWDK HYGFQLYQSD PSGNYGGWKA T CIGNNSAA AVSMLKQDYK EGEMTLKSAL ALAIKVLNKT MDVSKLSAEK VEIATLTREN GKTVIRVLKQ KEVEQLIKKH EE EEAKAER E

UniProtKB: Proteasome subunit alpha type-4

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Macromolecule #3: Proteasome subunit alpha type-7

MacromoleculeName: Proteasome subunit alpha type-7 / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 26.277986 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: YDRAITVFSP DGHLFQVEYA QEAVKKGSTA VGVRGRDIVV LGVEKKSVAK LQDERTVRKI CALDDNVCMA FAGLTADARI VINRARVEC QSHRLTVEDP VTVEYITRYI ASLKQRYTQS NGRRPFGISA LIVGFDFDGT PRLYQTDPSG TYHAWKANAI G RGAKSVRE ...String:
YDRAITVFSP DGHLFQVEYA QEAVKKGSTA VGVRGRDIVV LGVEKKSVAK LQDERTVRKI CALDDNVCMA FAGLTADARI VINRARVEC QSHRLTVEDP VTVEYITRYI ASLKQRYTQS NGRRPFGISA LIVGFDFDGT PRLYQTDPSG TYHAWKANAI G RGAKSVRE FLEKNYTDEA IETDDLTIKL VIKALLEVVQ SGGKNIELAV MRRDQSLKIL NPEEIEKYVA EIEKEK

UniProtKB: Proteasome subunit alpha type-7

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Macromolecule #4: Proteasome subunit alpha type-5

MacromoleculeName: Proteasome subunit alpha type-5 / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 26.322818 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MFLTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGI QTSEGVCLAV EKRITSPLME PSSIEKIVEI DAHIGCAMSG LIADAKTLI DKARVETQNH WFTYNETMTV ESVTQAVSNL ALQFGEEDAD PGAMSRPFGV ALLFGGVDEK GPQLFHMDPS G TFVQCDAR ...String:
MFLTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGI QTSEGVCLAV EKRITSPLME PSSIEKIVEI DAHIGCAMSG LIADAKTLI DKARVETQNH WFTYNETMTV ESVTQAVSNL ALQFGEEDAD PGAMSRPFGV ALLFGGVDEK GPQLFHMDPS G TFVQCDAR AIGSASEGAQ SSLQEVYHKS MTLKEAIKSS LIILKQVMEE KLNATNIELA TVQPGQNFHM FTKEELEEVI KD

UniProtKB: Proteasome subunit alpha type-5

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Macromolecule #5: Proteasome subunit alpha type-1

MacromoleculeName: Proteasome subunit alpha type-1 / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 27.163992 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK RAQSELAAHQ KKILHVDNHI GISIAGLTAD ARLLCNFMR QECLDSRFVF DRPLPVSRLV SLIGSKTQIP TQRYGRRPYG VGLLIAGYDD MGPHIFQTCP SANYFDCRAM S IGARSQSA ...String:
MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK RAQSELAAHQ KKILHVDNHI GISIAGLTAD ARLLCNFMR QECLDSRFVF DRPLPVSRLV SLIGSKTQIP TQRYGRRPYG VGLLIAGYDD MGPHIFQTCP SANYFDCRAM S IGARSQSA RTYLERHMSE FMECNLNELV KHGLRALRET LPAEQDLTTK NVSIGIVGKD LEFTIYDDDD VSPFLEGLEE RP Q

UniProtKB: Proteasome subunit alpha type-1

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Macromolecule #6: Proteasome subunit alpha type-3

MacromoleculeName: Proteasome subunit alpha type-3 / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 26.87067 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: GTGYDLSAST FSPDGRVFQV EYAMKAVENS STAIGIRCKD GVVFGVEKLV LSKLYEEGSN KRLFNVDRHV GMAVAGLLAD ARSLADIAR EEASNFRSNF GYNIPLKHLA DRVAMYVHAY TLYSAVRPFG CSFMLGSYSV NDGAQLYMID PSGVSYGYWG C AIGKARQA ...String:
GTGYDLSAST FSPDGRVFQV EYAMKAVENS STAIGIRCKD GVVFGVEKLV LSKLYEEGSN KRLFNVDRHV GMAVAGLLAD ARSLADIAR EEASNFRSNF GYNIPLKHLA DRVAMYVHAY TLYSAVRPFG CSFMLGSYSV NDGAQLYMID PSGVSYGYWG C AIGKARQA AKTEIEKLQM KEMTCRDIVK EVAKIIYIVH DEVKDKAFEL ELSWVGELTN GRHEIVPKDI REEAEKYAKE SL K

UniProtKB: Proteasome subunit alpha type-3

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Macromolecule #7: Proteasome subunit alpha type-6

MacromoleculeName: Proteasome subunit alpha type-6 / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 27.160178 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AINQGGLTSV AVRGKDCAVI VTQKKVPDKL LDSSTVTHLF KITENIGCVM TGMTADSRS QVQRARYEAA NWKYKYGYEI PVDMLCKRIA DISQVYTQNA EMRPLGCCMI LIGIDEEQGP QVYKCDPAGY Y CGFKATAA ...String:
MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AINQGGLTSV AVRGKDCAVI VTQKKVPDKL LDSSTVTHLF KITENIGCVM TGMTADSRS QVQRARYEAA NWKYKYGYEI PVDMLCKRIA DISQVYTQNA EMRPLGCCMI LIGIDEEQGP QVYKCDPAGY Y CGFKATAA GVKQTESTSF LEKKVKKKFD WTFEQTVETA ITCLSTVLSI DFKPSEIEVG VVTVENPKFR ILTEAEIDAH LV ALAE

UniProtKB: Proteasome subunit alpha type-6

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Macromolecule #8: Proteasome maturation protein

MacromoleculeName: Proteasome maturation protein / type: protein_or_peptide / ID: 8 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.804993 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
MNARGLGSEL KDSIPVTELS ASGPFESHDL LRKGFSCVKN ELLPSHPLEL SEKNFQLNQD KMNFSTLRNI QGLFAPLKLQ MEFKAVQQV QRLPFLSSSN LSLDVLRGND ETIGFEDILN DPSQSEVMGE PHLMVEYKLG LL

UniProtKB: Proteasome maturation protein

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Macromolecule #9: Proteasome assembly chaperone 1

MacromoleculeName: Proteasome assembly chaperone 1 / type: protein_or_peptide / ID: 9 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 32.891887 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MAATFFGEVV KAPCRAGTED EEEEEEGRRE TPEDREVRLQ LARKREVRLL RRQTKTSLEV SLLEKYPCSK FIIAIGNNAV AFLSSFVMN SGVWEEVGCA KLWNEWCRTT DTTHLSSTEA FCVFYHLKSN PSVFLCQCSC YVAEDQQYQW LEKVFGSCPR K NMQITILT ...String:
MAATFFGEVV KAPCRAGTED EEEEEEGRRE TPEDREVRLQ LARKREVRLL RRQTKTSLEV SLLEKYPCSK FIIAIGNNAV AFLSSFVMN SGVWEEVGCA KLWNEWCRTT DTTHLSSTEA FCVFYHLKSN PSVFLCQCSC YVAEDQQYQW LEKVFGSCPR K NMQITILT CRHVTDYKTS ESTGSLPSPF LRALKTQNFK DSACCPLLEQ PNIVHDLPAA VLSYCQVWKI PAILYLCYTD VM KLDLITV EAFKPILSTR SLKGLVKNIP QSTEILKKLM TTNEIQSNIY T

UniProtKB: Proteasome assembly chaperone 1

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Macromolecule #10: Proteasome assembly chaperone 2

MacromoleculeName: Proteasome assembly chaperone 2 / type: protein_or_peptide / ID: 10 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.423041 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MFVPCGESAP DLAGFTLLMP AVSVGNVGQL AMDLIISTLN MSKIGYFYTD CLVPMVGNNP YATTEGNSTE LSINAEVYSL PSRKLVALQ LRSIFIKYKS KPFCEKLLSW VKSSGCARVI VLSSSHSYQR NDLQLRSTPF RYLLTPSMQK SVQNKIKSLN W EEMEKSRC ...String:
MFVPCGESAP DLAGFTLLMP AVSVGNVGQL AMDLIISTLN MSKIGYFYTD CLVPMVGNNP YATTEGNSTE LSINAEVYSL PSRKLVALQ LRSIFIKYKS KPFCEKLLSW VKSSGCARVI VLSSSHSYQR NDLQLRSTPF RYLLTPSMQK SVQNKIKSLN W EEMEKSRC IPEIDDSEFC IRIPGGGITK TLYDESCSKE IQMAVLLKFV SEGDNIPDAL GLVEYLNEWL QILKPLSDDP TV SASRWKI PSSWRLLFGS GLPPALF

UniProtKB: Proteasome assembly chaperone 2

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Macromolecule #11: Proteasome subunit beta type-7

MacromoleculeName: Proteasome subunit beta type-7 / type: protein_or_peptide / ID: 11 / Number of copies: 2 / Enantiomer: LEVO / EC number: proteasome endopeptidase complex
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 28.292514 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: AAVSVYAPPV GGFSFDNCRR NAVLEADFAK RGYKLPKVRK TGTTIAGVVY KDGIVLGADT RATEGMVVAD KNCSKIHFIS PNIYCCGAG TAADTDMTTQ LISSNLELHS LSTGRLPRVV TANRMLKQML FRYQGYIGAA LVLGGVDVTG PHLYSIYPHG S TDKLPYVT ...String:
AAVSVYAPPV GGFSFDNCRR NAVLEADFAK RGYKLPKVRK TGTTIAGVVY KDGIVLGADT RATEGMVVAD KNCSKIHFIS PNIYCCGAG TAADTDMTTQ LISSNLELHS LSTGRLPRVV TANRMLKQML FRYQGYIGAA LVLGGVDVTG PHLYSIYPHG S TDKLPYVT MGSGSLAAMA VFEDKFRPDM EEEEAKNLVS EAIAAGIFND LGSGSNIDLC VISKNKLDFL RPYTVPNKKG TR LGRYRCE KGTTAVLTEK ITPLE

UniProtKB: Proteasome subunit beta type-7

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Macromolecule #12: Proteasome subunit beta type-3

MacromoleculeName: Proteasome subunit beta type-3 / type: protein_or_peptide / ID: 12 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 22.754623 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: IMSYNGGAVM AMKGKNCVAI AADRRFGIQA QMVTTDFQKI FPMGDRLYIG LAGLATDVQT VAQRLKFRLN LYELKEGRQI KPYTLMSMV ANLLYEKRFG PYYTEPVIAG LDPKTFKPFI CSLDLIGCPM VTDDFVVSGT CAEQMYGMCE SLWEPNMDPD H LFETISQA ...String:
IMSYNGGAVM AMKGKNCVAI AADRRFGIQA QMVTTDFQKI FPMGDRLYIG LAGLATDVQT VAQRLKFRLN LYELKEGRQI KPYTLMSMV ANLLYEKRFG PYYTEPVIAG LDPKTFKPFI CSLDLIGCPM VTDDFVVSGT CAEQMYGMCE SLWEPNMDPD H LFETISQA MLNAVDRDAV SGMGVIVHII EKDKITTRTL KARMD

UniProtKB: Proteasome subunit beta type-3

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Macromolecule #13: Proteasome subunit beta type-2

MacromoleculeName: Proteasome subunit beta type-2 / type: protein_or_peptide / ID: 13 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 22.462838 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MEYLIGIQGP DYVLVASDRV AASNIVQMKD DHDKMFKMSE KILLLCVGEA GDTVQFAEYI QKNVQLYKMR NGYELSPTAA ANFTRRNLA DCLRSRTPYH VNLLLAGYDE HEGPALYYMD YLAALAKAPF AAHGYGAFLT LSILDRYYTP TISRERAVEL L RKCLEELQ ...String:
MEYLIGIQGP DYVLVASDRV AASNIVQMKD DHDKMFKMSE KILLLCVGEA GDTVQFAEYI QKNVQLYKMR NGYELSPTAA ANFTRRNLA DCLRSRTPYH VNLLLAGYDE HEGPALYYMD YLAALAKAPF AAHGYGAFLT LSILDRYYTP TISRERAVEL L RKCLEELQ KRFILNLPTF SVRIIDKNGI HDLDNISFP

UniProtKB: Proteasome subunit beta type-2

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Macromolecule #14: Proteasome subunit beta type-5

MacromoleculeName: Proteasome subunit beta type-5 / type: protein_or_peptide / ID: 14 / Number of copies: 2 / Enantiomer: LEVO / EC number: proteasome endopeptidase complex
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 22.978012 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: PGIEMLHGTT TLAFKFRHGV IVAADSRATA GAYIASQTVK KVIEINPYLL GTMAGGAADC SFWERLLARQ CRIYELRNKE RISVAAASK LLANMVYQYK GMGLSMGTMI CGWDKRGPGL YYVDSEGNRI SGATFSVGSG SVYAYGVMDR GYSYDLEVEQ A YDLARRAI ...String:
PGIEMLHGTT TLAFKFRHGV IVAADSRATA GAYIASQTVK KVIEINPYLL GTMAGGAADC SFWERLLARQ CRIYELRNKE RISVAAASK LLANMVYQYK GMGLSMGTMI CGWDKRGPGL YYVDSEGNRI SGATFSVGSG SVYAYGVMDR GYSYDLEVEQ A YDLARRAI YQATYRDAYS GGAVNLYHVR EDGWIRVSSD NVADLHEKYS

UniProtKB: Proteasome subunit beta type-5

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Macromolecule #15: Proteasome subunit beta type-1

MacromoleculeName: Proteasome subunit beta type-1 / type: protein_or_peptide / ID: 15 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 23.421793 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: FSPYVFNGGT ILAIAGEDFA IVASDTRLSE GFSIHTRDSP KCYKLTDKTV IGCSGFHGDC LTLTKIIEAR LKMYKHSNNK AMTTGAIAA MLSTILYSRR FFPYYVYNII GGLDEEGKGA VYSFDPVGSY QRDSFKAGGS ASAMLQPLLD NQVGFKNMQN V EHVPLSLD ...String:
FSPYVFNGGT ILAIAGEDFA IVASDTRLSE GFSIHTRDSP KCYKLTDKTV IGCSGFHGDC LTLTKIIEAR LKMYKHSNNK AMTTGAIAA MLSTILYSRR FFPYYVYNII GGLDEEGKGA VYSFDPVGSY QRDSFKAGGS ASAMLQPLLD NQVGFKNMQN V EHVPLSLD RAMRLVKDVF ISAAERDVYT GDALRICIVT KEGIREETVS LRKD

UniProtKB: Proteasome subunit beta type-1

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Macromolecule #16: Proteasome subunit beta type-4

MacromoleculeName: Proteasome subunit beta type-4 / type: protein_or_peptide / ID: 16 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 23.159316 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MVTGTSVLGV KFEGGVVIAA DMLGSYGSLA RFRNISRIMR VNNSTMLGAS GDYADFQYLK QVLGQMVIDE ELLGDGHSYS PRAIHSWLT RAMYSRRSKM NPLWNTMVIG GYADGESFLG YVDMLGVAYE APSLATGYGA YLAQPLLREV LEKQPVLSQT E ARDLVERC ...String:
MVTGTSVLGV KFEGGVVIAA DMLGSYGSLA RFRNISRIMR VNNSTMLGAS GDYADFQYLK QVLGQMVIDE ELLGDGHSYS PRAIHSWLT RAMYSRRSKM NPLWNTMVIG GYADGESFLG YVDMLGVAYE APSLATGYGA YLAQPLLREV LEKQPVLSQT E ARDLVERC MRVLYYRDAR SYNRFQTATV TEKGVEIEGP LSTETNWDIA

UniProtKB: Proteasome subunit beta type-4

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Macromolecule #17: Proteasome subunit beta type-6

MacromoleculeName: Proteasome subunit beta type-6 / type: protein_or_peptide / ID: 17 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 21.158898 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: TTIMAVQFDG GVVLGADSRT TTGSYIANRV TDKLTPIHDR IFCCRSGSAA DTQAVADAVT YQLGFHSIEL NEPPLVHTAA SLFKEMCYR YREDLMAGII IAGWDPQEGG QGYSVPMGGM MVRQSFAIGG SGSSYIYGYV DATYREGMTK EECLQFTANA L ALAMERDG ...String:
TTIMAVQFDG GVVLGADSRT TTGSYIANRV TDKLTPIHDR IFCCRSGSAA DTQAVADAVT YQLGFHSIEL NEPPLVHTAA SLFKEMCYR YREDLMAGII IAGWDPQEGG QGYSVPMGGM MVRQSFAIGG SGSSYIYGYV DATYREGMTK EECLQFTANA L ALAMERDG SSGGVIRLAA IAESGVERQV LLGDQIPKF

UniProtKB: Proteasome subunit beta type-6

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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-PROPANE

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Electron microscopy

MicroscopeTFS GLACIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.6 µm / Nominal defocus min: 1.0 µm

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.89 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 59535
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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