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- EMDB-39332: Cryo-EM structure of human proteasome assembly intermediate half-... -

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Basic information

Entry
Database: EMDB / ID: EMD-39332
TitleCryo-EM structure of human proteasome assembly intermediate half-proteasome
Map data
Sample
  • Complex: Cryo-EM structure of human proteasome assembly intermediate half-proteasome
    • Protein or peptide: x 17 types
KeywordsProtein degradation / Proteasome / 20S proteasome / Assembly / Assembly chapreone / STRUCTURAL PROTEIN
Function / homology
Function and homology information


cerebellar granule cell precursor proliferation / purine ribonucleoside triphosphate binding / protein folding chaperone complex / Regulation of ornithine decarboxylase (ODC) / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / proteasome core complex / proteasome core complex assembly / Somitogenesis / mitotic spindle assembly checkpoint signaling ...cerebellar granule cell precursor proliferation / purine ribonucleoside triphosphate binding / protein folding chaperone complex / Regulation of ornithine decarboxylase (ODC) / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / proteasome core complex / proteasome core complex assembly / Somitogenesis / mitotic spindle assembly checkpoint signaling / proteasome binding / myofibril / immune system process / NF-kappaB binding / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasome assembly / threonine-type endopeptidase activity / chaperone-mediated protein complex assembly / proteasome core complex, alpha-subunit complex / proteasome complex / proteolysis involved in protein catabolic process / sarcomere / Regulation of activated PAK-2p34 by proteasome mediated degradation / 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 / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Degradation of DVL / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Dectin-1 mediated noncanonical NF-kB signaling / lipopolysaccharide binding / Degradation of AXIN / Hh mutants are degraded by ERAD / negative regulation of inflammatory response to antigenic stimulus / P-body / Activation of NF-kappaB in B cells / Degradation of GLI1 by the proteasome / Hedgehog ligand biogenesis / G2/M Checkpoints / Defective CFTR causes cystic fibrosis / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Autodegradation of the E3 ubiquitin ligase COP1 / Negative regulation of NOTCH4 signaling / 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 / 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 / MAPK6/MAPK4 signaling / : / Degradation of beta-catenin by the destruction complex / response to virus / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / ABC-family proteins mediated transport / CDK-mediated phosphorylation and removal of Cdc6 / CLEC7A (Dectin-1) signaling / SCF(Skp2)-mediated degradation of p27/p21 / Regulation of expression of SLITs and ROBOs / FCERI mediated NF-kB activation / nuclear matrix / Regulation of PTEN stability and activity / Interleukin-1 signaling / Orc1 removal from chromatin / Regulation of RAS by GAPs / positive regulation of NF-kappaB transcription factor activity / Regulation of RUNX2 expression and activity / Separation of Sister Chromatids / The role of GTSE1 in G2/M progression after G2 checkpoint / UCH proteinases / KEAP1-NFE2L2 pathway / Antigen processing: Ubiquitination & Proteasome degradation / Downstream TCR signaling / peptidase activity / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Neddylation / ER-Phagosome pathway / regulation of inflammatory response / secretory granule lumen / endopeptidase activity / molecular adaptor activity / response to oxidative stress / proteasome-mediated ubiquitin-dependent protein catabolic process / ficolin-1-rich granule lumen / Ub-specific processing proteases / nuclear speck / nuclear body / ciliary basal body / cilium / ribosome / cadherin binding
Similarity search - Function
Proteasome assembly chaperone 1 / Proteasome assembly chaperone 4 / Proteasome maturation factor Ump1 / Proteasome maturation factor UMP1 / Proteasome assembly chaperone 2, eukaryotic / 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 maturation factor Ump1 / Proteasome maturation factor UMP1 / Proteasome assembly chaperone 2, eukaryotic / 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 alpha6 / Proteasome subunit alpha5 / 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: 2.91 Å
AuthorsHan Y / Han Q / Tang Q / Zhang Y / Liu K
Funding support China, 2 items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2022ZD0213900 China
Ministry of Science and Technology (MoST, China)2022ZD0207400 China
CitationJournal: Sci Adv / Year: 2025
Title: Molecular basis for the stepwise and faithful maturation of the 20 proteasome.
Authors: Yaoyao Han / Qian Han / Qianqian Tang / Yixiao Zhang / Kai Liu /
Abstract: The proteasome degrades most superfluous and damaged proteins, and its decline is associated with many diseases. As the proteolytic unit, the 20 proteasome is assembled from 28 subunits assisted by ...The proteasome degrades most superfluous and damaged proteins, and its decline is associated with many diseases. As the proteolytic unit, the 20 proteasome is assembled from 28 subunits assisted by chaperones PAC1/2/3/4 and POMP; then, it undergoes the maturation process, in which the proteolytic sites are activated and the assembly chaperones are cleared. However, mechanisms governing the maturation remain elusive. Here, we captured endogenous maturation intermediates of human 20 proteasome, which are low abundance and highly dynamic, and determined their structures by cryo-electron microscopy. Through structure-based functional studies, we identified the key switches that remodel and activate the proteolytic sites. Our results also revealed that the POMP degradation is tightly controlled by a dual-checking mechanism, while the α5 subunit senses POMP degradation to induce PAC1/2 release, achieving the full maturation. These findings elucidate mechanisms directing and safeguarding the proteasome maturation and set basis for building proteasomes to counteract the decline of protein degradation in aging and disease.
History
DepositionFeb 29, 2024-
Header (metadata) releaseJan 15, 2025-
Map releaseJan 15, 2025-
UpdateJan 22, 2025-
Current statusJan 22, 2025Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_39332.png

Downloads & links

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Map

FileDownload / File: emd_39332.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.06 Å/pix.
x 300 pix.
= 316.5 Å		1.06 Å/pix.
x 300 pix.
= 316.5 Å		1.06 Å/pix.
x 300 pix.
= 316.5 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.055 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.592
Minimum - Maximum-3.506149 - 5.1281796
Average (Standard dev.)0.00010823732 (±0.16085765)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 316.49997 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_39332_half_map_1.map
Projections & Slices
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Density Histograms

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Half map: #1

Fileemd_39332_half_map_2.map
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Sample components

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Entire : Cryo-EM structure of human proteasome assembly intermediate half-...

EntireName: Cryo-EM structure of human proteasome assembly intermediate half-proteasome
Components
  • Complex: Cryo-EM structure of human proteasome assembly intermediate half-proteasome
    • 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 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
    • Protein or peptide: Proteasome assembly chaperone 1
    • Protein or peptide: Proteasome assembly chaperone 2
    • Protein or peptide: Proteasome maturation protein

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Supramolecule #1: Cryo-EM structure of human proteasome assembly intermediate half-...

SupramoleculeName: Cryo-EM structure of human proteasome assembly intermediate half-proteasome
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: 1 / Enantiomer: LEVO / EC number: proteasome endopeptidase complex
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 25.927535 KDa
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: 1 / Enantiomer: LEVO / EC number: proteasome endopeptidase complex
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.525842 KDa
SequenceString: MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGH AGTCLGILAN DGVLLAAERR NIHKLLDEVF FSEKIYKLNE DMACSVAGIT SDANVLTNE LRLIAQRYLL QYQEPIPCEQ LVTALCDIKQ AYTQFGGKRP FGVSLLYIGW DKHYGFQLYQ SDPSGNYGGW K ATCIGNNS ...String:
MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGH AGTCLGILAN DGVLLAAERR NIHKLLDEVF FSEKIYKLNE DMACSVAGIT SDANVLTNE LRLIAQRYLL QYQEPIPCEQ LVTALCDIKQ AYTQFGGKRP FGVSLLYIGW DKHYGFQLYQ SDPSGNYGGW K ATCIGNNS AAAVSMLKQD YKEGEMTLKS ALALAIKVLN KTMDVSKLSA EKVEIATLTR ENGKTVIRVL KQKEVEQLIK KH EEEEAKA EREKKEKEQK EKDK

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: 1 / Enantiomer: LEVO / EC number: proteasome endopeptidase complex
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 27.929891 KDa
SequenceString: MSYDRAITVF SPDGHLFQVE YAQEAVKKGS TAVGVRGRDI VVLGVEKKSV AKLQDERTVR KICALDDNVC MAFAGLTADA RIVINRARV ECQSHRLTVE DPVTVEYITR YIASLKQRYT QSNGRRPFGI SALIVGFDFD GTPRLYQTDP SGTYHAWKAN A IGRGAKSV ...String:
MSYDRAITVF SPDGHLFQVE YAQEAVKKGS TAVGVRGRDI VVLGVEKKSV AKLQDERTVR KICALDDNVC MAFAGLTADA RIVINRARV ECQSHRLTVE DPVTVEYITR YIASLKQRYT QSNGRRPFGI SALIVGFDFD GTPRLYQTDP SGTYHAWKAN A IGRGAKSV REFLEKNYTD EAIETDDLTI KLVIKALLEV VQSGGKNIEL AVMRRDQSLK ILNPEEIEKY VAEIEKEKEE NE KKKQKKA S

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: 1 / Enantiomer: LEVO / EC number: proteasome endopeptidase complex
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 26.435977 KDa
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 I

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: 1 / Enantiomer: LEVO / EC number: proteasome endopeptidase complex
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.595627 KDa
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 QRKAQPA QPADEPAEKA DEPMEH

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: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 28.469252 KDa
SequenceString: MSSIGTGYDL SASTFSPDGR VFQVEYAMKA VENSSTAIGI RCKDGVVFGV EKLVLSKLYE EGSNKRLFNV DRHVGMAVAG LLADARSLA DIAREEASNF RSNFGYNIPL KHLADRVAMY VHAYTLYSAV RPFGCSFMLG SYSVNDGAQL YMIDPSGVSY G YWGCAIGK ...String:
MSSIGTGYDL SASTFSPDGR VFQVEYAMKA VENSSTAIGI RCKDGVVFGV EKLVLSKLYE EGSNKRLFNV DRHVGMAVAG LLADARSLA DIAREEASNF RSNFGYNIPL KHLADRVAMY VHAYTLYSAV RPFGCSFMLG SYSVNDGAQL YMIDPSGVSY G YWGCAIGK ARQAAKTEIE KLQMKEMTCR DIVKEVAKII YIVHDEVKDK AFELELSWVG ELTNGRHEIV PKDIREEAEK YA KESLKEE DESDDDNM

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: 1 / Enantiomer: LEVO / EC number: proteasome endopeptidase complex
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 27.432459 KDa
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 ALAERD

UniProtKB: Proteasome subunit alpha type-6

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Macromolecule #8: Proteasome subunit beta type-7

MacromoleculeName: Proteasome subunit beta type-7 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO / EC number: proteasome endopeptidase complex
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 30.000418 KDa
SequenceString: MAAVSVYAPP VGGFSFDNCR RNAVLEADFA KRGYKLPKVR KTGTTIAGVV YKDGIVLGAD TRATEGMVVA DKNCSKIHFI SPNIYCCGA GTAADTDMTT QLISSNLELH SLSTGRLPRV VTANRMLKQM LFRYQGYIGA ALVLGGVDVT GPHLYSIYPH G STDKLPYV ...String:
MAAVSVYAPP VGGFSFDNCR RNAVLEADFA KRGYKLPKVR KTGTTIAGVV YKDGIVLGAD TRATEGMVVA DKNCSKIHFI SPNIYCCGA GTAADTDMTT QLISSNLELH SLSTGRLPRV VTANRMLKQM LFRYQGYIGA ALVLGGVDVT GPHLYSIYPH G STDKLPYV TMGSGSLAAM AVFEDKFRPD MEEEEAKNLV SEAIAAGIFN DLGSGSNIDL CVISKNKLDF LRPYTVPNKK GT RLGRYRC EKGTTAVLTE KITPLEIEVL EETVQTMDTS

UniProtKB: Proteasome subunit beta type-7

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Macromolecule #9: Proteasome subunit beta type-3

MacromoleculeName: Proteasome subunit beta type-3 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO / EC number: proteasome endopeptidase complex
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 22.972896 KDa
SequenceString: MSIMSYNGGA VMAMKGKNCV AIAADRRFGI QAQMVTTDFQ KIFPMGDRLY IGLAGLATDV QTVAQRLKFR LNLYELKEGR QIKPYTLMS MVANLLYEKR FGPYYTEPVI AGLDPKTFKP FICSLDLIGC PMVTDDFVVS GTCAEQMYGM CESLWEPNMD P DHLFETIS ...String:
MSIMSYNGGA VMAMKGKNCV AIAADRRFGI QAQMVTTDFQ KIFPMGDRLY IGLAGLATDV QTVAQRLKFR LNLYELKEGR QIKPYTLMS MVANLLYEKR FGPYYTEPVI AGLDPKTFKP FICSLDLIGC PMVTDDFVVS GTCAEQMYGM CESLWEPNMD P DHLFETIS QAMLNAVDRD AVSGMGVIVH IIEKDKITTR TLKARMD

UniProtKB: Proteasome subunit beta type-3

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Macromolecule #10: Proteasome subunit beta type-2

MacromoleculeName: Proteasome subunit beta type-2 / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO / EC number: proteasome endopeptidase complex
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 22.864277 KDa
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 HDLDNISFPK QGS

UniProtKB: Proteasome subunit beta type-2

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Macromolecule #11: Proteasome subunit beta type-5

MacromoleculeName: Proteasome subunit beta type-5 / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO / EC number: proteasome endopeptidase complex
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 28.510248 KDa
SequenceString: MALASVLERP LPVNQRGFFG LGGRADLLDL GPGSLSDGLS LAAPGWGVPE EPGIEMLHGT TTLAFKFRHG VIVAADSRAT AGAYIASQT VKKVIEINPY LLGTMAGGAA DCSFWERLLA RQCRIYELRN KERISVAAAS KLLANMVYQY KGMGLSMGTM I CGWDKRGP ...String:
MALASVLERP LPVNQRGFFG LGGRADLLDL GPGSLSDGLS LAAPGWGVPE EPGIEMLHGT TTLAFKFRHG VIVAADSRAT AGAYIASQT VKKVIEINPY LLGTMAGGAA DCSFWERLLA RQCRIYELRN KERISVAAAS KLLANMVYQY KGMGLSMGTM I CGWDKRGP GLYYVDSEGN RISGATFSVG SGSVYAYGVM DRGYSYDLEV EQAYDLARRA IYQATYRDAY SGGAVNLYHV RE DGWIRVS SDNVADLHEK YSGSTP

UniProtKB: Proteasome subunit beta type-5

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Macromolecule #12: Proteasome subunit beta type-1

MacromoleculeName: Proteasome subunit beta type-1 / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO / EC number: proteasome endopeptidase complex
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 26.522396 KDa
SequenceString: MLSSTAMYSA PGRDLGMEPH RAAGPLQLRF SPYVFNGGTI LAIAGEDFAI VASDTRLSEG FSIHTRDSPK CYKLTDKTVI GCSGFHGDC LTLTKIIEAR LKMYKHSNNK AMTTGAIAAM LSTILYSRRF FPYYVYNIIG GLDEEGKGAV YSFDPVGSYQ R DSFKAGGS ...String:
MLSSTAMYSA PGRDLGMEPH RAAGPLQLRF SPYVFNGGTI LAIAGEDFAI VASDTRLSEG FSIHTRDSPK CYKLTDKTVI GCSGFHGDC LTLTKIIEAR LKMYKHSNNK AMTTGAIAAM LSTILYSRRF FPYYVYNIIG GLDEEGKGAV YSFDPVGSYQ R DSFKAGGS ASAMLQPLLD NQVGFKNMQN VEHVPLSLDR AMRLVKDVFI SAAERDVYTG DALRICIVTK EGIREETVSL RK D

UniProtKB: Proteasome subunit beta type-1

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Macromolecule #13: Proteasome subunit beta type-4

MacromoleculeName: Proteasome subunit beta type-4 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 27.942734 KDa
SequenceString: MEAFLGSRSG LWAGGPAPGQ FYRIPSTPDS FMDPASALYR GPITRTQNPM VTGTSVLGVK FEGGVVIAAD MLGSYGSLAR FRNISRIMR VNNSTMLGAS GDYADFQYLK QVLGQMVIDE ELLGDGHSYS PRAIHSWLTR AMYSRRSKMN PLWNTMVIGG Y ADGESFLG ...String:
MEAFLGSRSG LWAGGPAPGQ FYRIPSTPDS FMDPASALYR GPITRTQNPM VTGTSVLGVK FEGGVVIAAD MLGSYGSLAR FRNISRIMR VNNSTMLGAS GDYADFQYLK QVLGQMVIDE ELLGDGHSYS PRAIHSWLTR AMYSRRSKMN PLWNTMVIGG Y ADGESFLG YVDMLGVAYE APSLATGYGA YLAQPLLREV LEKQPVLSQT EARDLVERCM RVLYYRDARS YNRFQIATVT EK GVEIEGP LSTETN

UniProtKB: Proteasome subunit beta type-4

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Macromolecule #14: Proteasome subunit beta type-6

MacromoleculeName: Proteasome subunit beta type-6 / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO / EC number: proteasome endopeptidase complex
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 25.377652 KDa
SequenceString: MAATLLAARG AGPAPAWGPE AFTPDWESRE VSTGTTIMAV QFDGGVVLGA DSRTTTGSYI ANRVTDKLTP IHDRIFCCRS GSAADTQAV ADAVTYQLGF HSIELNEPPL VHTAASLFKE MCYRYREDLM AGIIIAGWDP QEGGQVYSVP MGGMMVRQSF A IGGSGSSY ...String:
MAATLLAARG AGPAPAWGPE AFTPDWESRE VSTGTTIMAV QFDGGVVLGA DSRTTTGSYI ANRVTDKLTP IHDRIFCCRS GSAADTQAV ADAVTYQLGF HSIELNEPPL VHTAASLFKE MCYRYREDLM AGIIIAGWDP QEGGQVYSVP MGGMMVRQSF A IGGSGSSY IYGYVDATYR EGMTKEECLQ FTANALALAM ERDGSSGGVI RLAAIAESGV ERQVLLGDQI PKFAVATLPP A

UniProtKB: Proteasome subunit beta type-6

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Macromolecule #15: Proteasome assembly chaperone 1

MacromoleculeName: Proteasome assembly chaperone 1 / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 32.891887 KDa
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 #16: Proteasome assembly chaperone 2

MacromoleculeName: Proteasome assembly chaperone 2 / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.423041 KDa
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 #17: Proteasome maturation protein

MacromoleculeName: Proteasome maturation protein / type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.804993 KDa
SequenceString:
MNARGLGSEL KDSIPVTELS ASGPFESHDL LRKGFSCVKN ELLPSHPLEL SEKNFQLNQD KMNFSTLRNI QGLFAPLKLQ MEFKAVQQV QRLPFLSSSN LSLDVLRGND ETIGFEDILN DPSQSEVMGE PHLMVEYKLG LL

UniProtKB: Proteasome maturation protein

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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: 7.9
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TECNAI 12
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 49.41 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 1.4000000000000001 µm

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Image processing

Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

5le5

Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.91 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 310562
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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