[English] 日本語
Yorodumi
- EMDB-22259: Human 20S proteasome bound to an engineered 11S (PA26) activator -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-22259
TitleHuman 20S proteasome bound to an engineered 11S (PA26) activator
Map dataSharpened and masked
Sample
  • Complex: PA26-bound proteasome
    • Complex: Proteasome
      • Protein or peptide: x 14 types
    • Complex: mutant PA26
      • Protein or peptide: x 1 types
Keywords11S-bound / 20S proteasome / HYDROLASE
Function / homology
Function and homology information


proteasome activator complex / purine ribonucleoside triphosphate binding / regulation of endopeptidase activity / proteasome core complex / Regulation of ornithine decarboxylase (ODC) / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis / immune system process / myofibril / NF-kappaB binding ...proteasome activator complex / purine ribonucleoside triphosphate binding / regulation of endopeptidase activity / proteasome core complex / Regulation of ornithine decarboxylase (ODC) / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis / immune system process / myofibril / NF-kappaB binding / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasome core complex, alpha-subunit complex / threonine-type endopeptidase activity / regulation of proteasomal protein catabolic process / negative regulation of inflammatory response to antigenic stimulus / : / sarcomere / proteasome complex / Regulation of activated PAK-2p34 by proteasome mediated degradation / ciliary basal body / proteolysis involved in protein catabolic process / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / Asymmetric localization of PCP proteins / SCF-beta-TrCP mediated degradation of Emi1 / AUF1 (hnRNP D0) binds and destabilizes mRNA / NIK-->noncanonical NF-kB signaling / Ubiquitin-dependent degradation of Cyclin D / TNFR2 non-canonical NF-kB pathway / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / Degradation of DVL / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Dectin-1 mediated noncanonical NF-kB signaling / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Hh mutants are degraded by ERAD / lipopolysaccharide binding / Degradation of AXIN / Degradation of GLI1 by the proteasome / Activation of NF-kappaB in B cells / Hedgehog ligand biogenesis / Defective CFTR causes cystic fibrosis / Negative regulation of NOTCH4 signaling / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / G2/M Checkpoints / Vif-mediated degradation of APOBEC3G / Autodegradation of the E3 ubiquitin ligase COP1 / Hedgehog 'on' state / Regulation of RUNX3 expression and activity / 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 / P-body / MAPK6/MAPK4 signaling / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / response to virus / Degradation of beta-catenin by the destruction complex / ABC-family proteins mediated transport / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / response to organic cyclic compound / 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 / nuclear matrix / FCERI mediated NF-kB activation / Regulation of PTEN stability and activity / Interleukin-1 signaling / Orc1 removal from chromatin / Regulation of RAS by GAPs / Separation of Sister Chromatids / Regulation of RUNX2 expression and activity / UCH proteinases / The role of GTSE1 in G2/M progression after G2 checkpoint / KEAP1-NFE2L2 pathway / Antigen processing: Ubiquitination & Proteasome degradation / Downstream TCR signaling / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Neddylation / peptidase activity / positive regulation of NF-kappaB transcription factor activity / ER-Phagosome pathway / regulation of inflammatory response / postsynapse / proteasome-mediated ubiquitin-dependent protein catabolic process / secretory granule lumen / endopeptidase activity / ficolin-1-rich granule lumen / response to oxidative stress / nuclear body / ribosome / Ub-specific processing proteases / cadherin binding / intracellular membrane-bounded organelle / centrosome / ubiquitin protein ligase binding / synapse / Neutrophil degranulation / mitochondrion
Similarity search - Function
Proteasome activator PA28, C-terminal domain / Proteasome activator superfamily / Proteasome activator PA28, C-terminal domain superfamily / Proteasome activator PA28, C-terminal / 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 activator PA28, C-terminal domain / Proteasome activator superfamily / Proteasome activator PA28, C-terminal domain superfamily / Proteasome activator PA28, C-terminal / 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 alpha-type subunit / Proteasome alpha-type subunit profile. / Proteasome B-type subunit / Proteasome beta-type subunit profile. / Proteasome subunit / Proteasome, subunit alpha/beta / Nucleophile aminohydrolases, N-terminal
Similarity search - Domain/homology
Proteasome subunit alpha type-7 / 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 alpha type-7 / 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 subunit beta type-7 / Proteasome activator protein PA26
Similarity search - Component
Biological speciesHomo sapiens (human) / Trypanosoma brucei (eukaryote)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.0 Å
Authorsde la Pena AH / Opoku-Nsiah KA / Williams SK / Chopra N / Sali A / Gestwicki JE / Lander GC
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)DP2-EB020402 United States
American Cancer Society132279-PF-18-189-01- DMC United States
CitationJournal: Nat Commun / Year: 2022
Title: The YΦ motif defines the structure-activity relationships of human 20S proteasome activators.
Authors: Kwadwo A Opoku-Nsiah / Andres H de la Pena / Sarah K Williams / Nikita Chopra / Andrej Sali / Gabriel C Lander / Jason E Gestwicki /
Abstract: The 20S proteasome (20S) facilitates turnover of most eukaryotic proteins. Substrate entry into the 20S first requires opening of gating loops through binding of HbYX motifs that are present at the C- ...The 20S proteasome (20S) facilitates turnover of most eukaryotic proteins. Substrate entry into the 20S first requires opening of gating loops through binding of HbYX motifs that are present at the C-termini of certain proteasome activators (PAs). The HbYX motif has been predominantly characterized in the archaeal 20S, whereas little is known about the sequence preferences of the human 20S (h20S). Here, we synthesize and screen ~120 HbYX-like peptides, revealing unexpected differences from the archaeal system and defining the h20S recognition sequence as the Y-F/Y (YФ) motif. To gain further insight, we create a functional chimera of the optimized sequence, NLSYYT, fused to the model activator, PA26. A cryo-EM structure of PA26-h20S is used to identify key interactions, including non-canonical contacts and gate-opening mechanisms. Finally, we demonstrate that the YФ sequence preferences are tuned by valency, allowing multivalent PAs to sample greater sequence space. These results expand the model for termini-mediated gating and provide a template for the design of h20S activators.
History
DepositionJun 30, 2020-
Header (metadata) releaseJul 22, 2020-
Map releaseJul 22, 2020-
UpdateMay 15, 2024-
Current statusMay 15, 2024Processing site: RCSB / Status: Released

-
Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.08
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 0.08
  • Imaged by UCSF Chimera
  • Download
  • Surface view with fitted model
  • Atomic models: PDB-6xmj
  • Surface level: 0.08
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_22259.png

Downloads & links

-
Map

FileDownload / File: emd_22259.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationSharpened and masked
Voxel sizeX=Y=Z: 1.03 Å
Density
Contour LevelBy AUTHOR: 0.08 / Movie #1: 0.08
Minimum - Maximum-0.21817514 - 0.37889218
Average (Standard dev.)0.000872798 (±0.016095666)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 263.68 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.031.031.03
M x/y/z256256256
origin x/y/z0.0000.0000.000
length x/y/z263.680263.680263.680
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ368368368
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS256256256
D min/max/mean-0.2180.3790.001

-
Supplemental data

-
Mask #1

Fileemd_22259_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Half map: Unfiltered half-map 1

Fileemd_22259_half_map_1.map
AnnotationUnfiltered half-map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Half map: Unfiltered half-map 2

Fileemd_22259_half_map_2.map
AnnotationUnfiltered half-map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Sample components

+
Entire : PA26-bound proteasome

EntireName: PA26-bound proteasome
Components
  • Complex: PA26-bound proteasome
    • Complex: Proteasome
      • Protein or peptide: Proteasome subunit alpha type-6
      • 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 beta 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
    • Complex: mutant PA26
      • Protein or peptide: Proteasome activator protein PA26

+
Supramolecule #1: PA26-bound proteasome

SupramoleculeName: PA26-bound proteasome / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all

+
Supramolecule #2: Proteasome

SupramoleculeName: Proteasome / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#14
Source (natural)Organism: Homo sapiens (human)

+
Supramolecule #3: mutant PA26

SupramoleculeName: mutant PA26 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #15
Source (natural)Organism: Trypanosoma brucei (eukaryote)

+
Macromolecule #1: Proteasome subunit alpha type-6

MacromoleculeName: Proteasome subunit alpha type-6 / 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: 27.186174 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: SRGSSAGFDR HITIFSPEGR LYQVEYAFKA INQGGLTSVA VRGKDCAVIV TQKKVPDKLL DSSTVTHLFK ITENIGCVMT GMTADSRSQ VQRARYEAAN WKYKYGYEIP VDMLCKRIAD ISQVYTQNAE MRPLGCCMIL IGIDEEQGPQ VYKCDPAGYY C GFKATAAG ...String:
SRGSSAGFDR HITIFSPEGR LYQVEYAFKA INQGGLTSVA VRGKDCAVIV TQKKVPDKLL DSSTVTHLFK ITENIGCVMT GMTADSRSQ VQRARYEAAN WKYKYGYEIP VDMLCKRIAD ISQVYTQNAE MRPLGCCMIL IGIDEEQGPQ VYKCDPAGYY C GFKATAAG VKQTESTSFL EKKVKKKFDW TFEQTVETAI TCLSTVLSID FKPSEIEVGV VTVENPKFRI LTEAEIDAHL VA LAER

UniProtKB: Proteasome subunit alpha type-6

+
Macromolecule #2: Proteasome subunit alpha type-2

MacromoleculeName: Proteasome subunit alpha type-2 / 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: 25.796338 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: AERGYSFSLT TFSPSGKLVQ IEYALAAVAG GAPSVGIKAA NGVVLATEKK QKSILYDERS VHKVEPITKH IGLVYSGMGP DYRVLVHRA RKLAQQYYLV YQEPIPTAQL VQRVASVMQE YTQSGGVRPF GVSLLICGWN EGRPYLFQSD PSGAYFAWKA T AMGKNYVN ...String:
AERGYSFSLT TFSPSGKLVQ IEYALAAVAG GAPSVGIKAA NGVVLATEKK QKSILYDERS VHKVEPITKH IGLVYSGMGP DYRVLVHRA RKLAQQYYLV YQEPIPTAQL VQRVASVMQE YTQSGGVRPF GVSLLICGWN EGRPYLFQSD PSGAYFAWKA T AMGKNYVN GKTFLEKRYN EDLELEDAIH TAILTLKESF EGQMTEDNIE VGICNEAGFR RLTPTEVKDY LAAIA

UniProtKB: Proteasome subunit alpha type-2

+
Macromolecule #3: Proteasome subunit alpha type-4

MacromoleculeName: Proteasome subunit alpha type-4 / 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: 28.118189 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: SRRYDSRTTI FSPEGRLYQV EYAMEAIGHA GTCLGILAND GVLLAAERRN IHKLLDEVFF SEKIYKLNED MACSVAGITS DANVLTNEL RLIAQRYLLQ YQEPIPCEQL VTALCDIKQA YTQFGGKRPF GVSLLYIGWD KHYGFQLYQS DPSGNYGGWK A TCIGNNSA ...String:
SRRYDSRTTI FSPEGRLYQV EYAMEAIGHA GTCLGILAND GVLLAAERRN IHKLLDEVFF SEKIYKLNED MACSVAGITS DANVLTNEL RLIAQRYLLQ YQEPIPCEQL VTALCDIKQA YTQFGGKRPF GVSLLYIGWD KHYGFQLYQS DPSGNYGGWK A TCIGNNSA AAVSMLKQDY KEGEMTLKSA LALAIKVLNK TMDVSKLSAE KVEIATLTRE NGKTVIRVLK QKEVEQLIKK HE EEEAKAE REK

UniProtKB: Proteasome subunit alpha type-4

+
Macromolecule #4: Proteasome subunit alpha type-7

MacromoleculeName: Proteasome subunit alpha type-7 / 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: 27.382178 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: SYDRAITVFS PDGHLFQVEY AQEAVKKGST AVGVRGRDIV VLGVEKKSVA KLQDERTVRK ICALDDNVCM AFAGLTADAR IVINRARVE CQSHRLTVED PVTVEYITRY IASLKQRYTQ SNGRRPFGIS ALIVGFDFDG TPRLYQTDPS GTYHAWKANA I GRGAKSVR ...String:
SYDRAITVFS PDGHLFQVEY AQEAVKKGST AVGVRGRDIV VLGVEKKSVA KLQDERTVRK ICALDDNVCM AFAGLTADAR IVINRARVE CQSHRLTVED PVTVEYITRY IASLKQRYTQ SNGRRPFGIS ALIVGFDFDG TPRLYQTDPS GTYHAWKANA I GRGAKSVR EFLEKNYTDE AIETDDLTIK LVIKALLEVV QSGGKNIELA VMRRDQSLKI LNPEEIEKYV AEIEKEKEEN EK KKQ

UniProtKB: Proteasome subunit alpha type-7

+
Macromolecule #5: Proteasome subunit alpha type-5

MacromoleculeName: Proteasome subunit alpha type-5 / 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: 25.569957 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: YDRGVNTFSP EGRLFQVEYA IEAIKLGSTA IGIQTSEGVC LAVEKRITSP LMEPSSIEKI VEIDAHIGCA MSGLIADAKT LIDKARVET QNHWFTYNET MTVESVTQAV SNLALQFGEE DADPGAMSRP FGVALLFGGV DEKGPQLFHM DPSGTFVQCD A RAIGSASE ...String:
YDRGVNTFSP EGRLFQVEYA IEAIKLGSTA IGIQTSEGVC LAVEKRITSP LMEPSSIEKI VEIDAHIGCA MSGLIADAKT LIDKARVET QNHWFTYNET MTVESVTQAV SNLALQFGEE DADPGAMSRP FGVALLFGGV DEKGPQLFHM DPSGTFVQCD A RAIGSASE GAQSSLQEVY HKSMTLKEAI KSSLIILKQV MEEKLNATNI ELATVQPGQN FHMFTKEELE EVIKDI

UniProtKB: Proteasome subunit alpha type-5

+
Macromolecule #6: Proteasome subunit alpha type-1

MacromoleculeName: Proteasome subunit alpha type-1 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO / EC number: proteasome endopeptidase complex
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 26.728428 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: NQYDNDVTVW SPQGRIHQIE YAMEAVKQGS ATVGLKSKTH AVLVALKRAQ SELAAHQKKI LHVDNHIGIS IAGLTADARL LCNFMRQEC LDSRFVFDRP LPVSRLVSLI GSKTQIPTQR YGRRPYGVGL LIAGYDDMGP HIFQTCPSAN YFDCRAMSIG A RSQSARTY ...String:
NQYDNDVTVW SPQGRIHQIE YAMEAVKQGS ATVGLKSKTH AVLVALKRAQ SELAAHQKKI LHVDNHIGIS IAGLTADARL LCNFMRQEC LDSRFVFDRP LPVSRLVSLI GSKTQIPTQR YGRRPYGVGL LIAGYDDMGP HIFQTCPSAN YFDCRAMSIG A RSQSARTY LERHMSEFME CNLNELVKHG LRALRETLPA EQDLTTKNVS IGIVGKDLEF TIYDDDDVSP FLEGLEERPQ

UniProtKB: Proteasome subunit alpha type-1

+
Macromolecule #7: Proteasome subunit alpha type-3

MacromoleculeName: Proteasome subunit alpha type-3 / 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: 27.2871 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: SSIGTGYDLS ASTFSPDGRV FQVEYAMKAV ENSSTAIGIR CKDGVVFGVE KLVLSKLYEE GSNKRLFNVD RHVGMAVAGL LADARSLAD IAREEASNFR SNFGYNIPLK HLADRVAMYV HAYTLYSAVR PFGCSFMLGS YSVNDGAQLY MIDPSGVSYG Y WGCAIGKA ...String:
SSIGTGYDLS ASTFSPDGRV FQVEYAMKAV ENSSTAIGIR CKDGVVFGVE KLVLSKLYEE GSNKRLFNVD RHVGMAVAGL LADARSLAD IAREEASNFR SNFGYNIPLK HLADRVAMYV HAYTLYSAVR PFGCSFMLGS YSVNDGAQLY MIDPSGVSYG Y WGCAIGKA RQAAKTEIEK LQMKEMTCRD IVKEVAKIIY IVHDEVKDKA FELELSWVGE LTNGRHEIVP KDIREEAEKY AK ESLKE

UniProtKB: Proteasome subunit alpha type-3

+
Macromolecule #8: Proteasome subunit beta type-6

MacromoleculeName: Proteasome subunit beta type-6 / 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: 21.656527 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: TTIMAVQFDG GVVLGADSRT TTGSYIANRV TDKLTPIHDR IFCCRSGSAA DTQAVADAVT YQLGFHSIEL NEPPLVHTAA SLFKEMCYR YREDLMAGII IAGWDPQEGG QVYSVPMGGM MVRQSFAIGG SGSSYIYGYV DATYREGMTK EECLQFTANA L ALAMERDG ...String:
TTIMAVQFDG GVVLGADSRT TTGSYIANRV TDKLTPIHDR IFCCRSGSAA DTQAVADAVT YQLGFHSIEL NEPPLVHTAA SLFKEMCYR YREDLMAGII IAGWDPQEGG QVYSVPMGGM MVRQSFAIGG SGSSYIYGYV DATYREGMTK EECLQFTANA L ALAMERDG SSGGVIRLAA IAESGVERQV LLGDQIPKFA VATL

UniProtKB: Proteasome subunit beta type-6

+
Macromolecule #9: Proteasome subunit beta type-7

MacromoleculeName: Proteasome subunit beta type-7 / 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: 23.745256 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: TTIAGVVYKD GIVLGADTRA TEGMVVADKN CSKIHFISPN IYCCGAGTAA DTDMTTQLIS SNLELHSLST GRLPRVVTAN RMLKQMLFR YQGYIGAALV LGGVDVTGPH LYSIYPHGST DKLPYVTMGS GSLAAMAVFE DKFRPDMEEE EAKNLVSEAI A AGIFNDLG ...String:
TTIAGVVYKD GIVLGADTRA TEGMVVADKN CSKIHFISPN IYCCGAGTAA DTDMTTQLIS SNLELHSLST GRLPRVVTAN RMLKQMLFR YQGYIGAALV LGGVDVTGPH LYSIYPHGST DKLPYVTMGS GSLAAMAVFE DKFRPDMEEE EAKNLVSEAI A AGIFNDLG SGSNIDLCVI SKNKLDFLRP YTVPNKKGTR LGRYRCEKGT TAVLTEKITP LE

UniProtKB: Proteasome subunit beta type-7

+
Macromolecule #10: Proteasome subunit beta type-3

MacromoleculeName: Proteasome subunit beta type-3 / 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: 22.841701 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: SIMSYNGGAV MAMKGKNCVA IAADRRFGIQ AQMVTTDFQK IFPMGDRLYI GLAGLATDVQ TVAQRLKFRL NLYELKEGRQ IKPYTLMSM VANLLYEKRF GPYYTEPVIA GLDPKTFKPF ICSLDLIGCP MVTDDFVVSG TCAEQMYGMC ESLWEPNMDP D HLFETISQ ...String:
SIMSYNGGAV MAMKGKNCVA IAADRRFGIQ AQMVTTDFQK IFPMGDRLYI GLAGLATDVQ TVAQRLKFRL NLYELKEGRQ IKPYTLMSM VANLLYEKRF GPYYTEPVIA GLDPKTFKPF ICSLDLIGCP MVTDDFVVSG TCAEQMYGMC ESLWEPNMDP D HLFETISQ AMLNAVDRDA VSGMGVIVHI IEKDKITTRT LKARMD

UniProtKB: Proteasome subunit beta type-3

+
Macromolecule #11: Proteasome subunit beta type-2

MacromoleculeName: Proteasome subunit beta type-2 / 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: 22.720146 KDa
Recombinant expressionOrganism: Homo sapiens (human)
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 Q

UniProtKB: Proteasome subunit beta type-2

+
Macromolecule #12: Proteasome subunit beta type-5

MacromoleculeName: Proteasome subunit beta type-5 / 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: 22.199072 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: TTTLAFKFRH GVIVAADSRA TAGAYIASQT VKKVIEINPY LLGTMAGGAA DCSFWERLLA RQCRIYELRN KERISVAAAS KLLANMVYQ YKGMGLSMGT MICGWDKRGP GLYYVDSEGN RISGATFSVG SGSVYAYGVM DRGYSYDLEV EQAYDLARRA I YQATYRDA ...String:
TTTLAFKFRH GVIVAADSRA TAGAYIASQT VKKVIEINPY LLGTMAGGAA DCSFWERLLA RQCRIYELRN KERISVAAAS KLLANMVYQ YKGMGLSMGT MICGWDKRGP GLYYVDSEGN RISGATFSVG SGSVYAYGVM DRGYSYDLEV EQAYDLARRA I YQATYRDA YSGGAVNLYH VREDGWIRVS SDNVADLHEK YSG

UniProtKB: Proteasome subunit beta type-5

+
Macromolecule #13: Proteasome subunit beta type-1

MacromoleculeName: Proteasome subunit beta type-1 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO / EC number: proteasome endopeptidase complex
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 23.578986 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: RFSPYVFNGG TILAIAGEDF AIVASDTRLS EGFSIHTRDS PKCYKLTDKT VIGCSGFHGD CLTLTKIIEA RLKMYKHSNN KAMTTGAIA AMLSTILYSR RFFPYYVYNI IGGLDEEGKG AVYSFDPVGS YQRDSFKAGG SASAMLQPLL DNQVGFKNMQ N VEHVPLSL ...String:
RFSPYVFNGG TILAIAGEDF AIVASDTRLS EGFSIHTRDS PKCYKLTDKT VIGCSGFHGD CLTLTKIIEA RLKMYKHSNN KAMTTGAIA AMLSTILYSR RFFPYYVYNI IGGLDEEGKG AVYSFDPVGS YQRDSFKAGG SASAMLQPLL DNQVGFKNMQ N VEHVPLSL DRAMRLVKDV FISAAERDVY TGDALRICIV TKEGIREETV SLRKD

UniProtKB: Proteasome subunit beta type-1

+
Macromolecule #14: Proteasome subunit beta type-4

MacromoleculeName: Proteasome subunit beta type-4 / 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: 24.138453 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: TQNPMVTGTS VLGVKFEGGV VIAADMLGSY GSLARFRNIS RIMRVNNSTM LGASGDYADF QYLKQVLGQM VIDEELLGDG HSYSPRAIH SWLTRAMYSR RSKMNPLWNT MVIGGYADGE SFLGYVDMLG VAYEAPSLAT GYGAYLAQPL LREVLEKQPV L SQTEARDL ...String:
TQNPMVTGTS VLGVKFEGGV VIAADMLGSY GSLARFRNIS RIMRVNNSTM LGASGDYADF QYLKQVLGQM VIDEELLGDG HSYSPRAIH SWLTRAMYSR RSKMNPLWNT MVIGGYADGE SFLGYVDMLG VAYEAPSLAT GYGAYLAQPL LREVLEKQPV L SQTEARDL VERCMRVLYY RDARSYNRFQ IATVTEKGVE IEGPLSTETN WDIAHMISG

UniProtKB: Proteasome subunit beta type-4

+
Macromolecule #15: Proteasome activator protein PA26

MacromoleculeName: Proteasome activator protein PA26 / type: protein_or_peptide / ID: 15 / Number of copies: 7 / Enantiomer: LEVO
Source (natural)Organism: Trypanosoma brucei (eukaryote)
Molecular weightTheoretical: 24.959373 KDa
Recombinant expressionOrganism: Escherichia coli BL21 (bacteria)
SequenceString: KRAALIQNLR DSYTETSSFA VIEEWAAGTL QEIEGIAKAA AEAHGVIRNS TYGRAQAEKS PEQLLGVLQR YQDLCHNVYC QAETIRTVI AIRIPEHKEA DNLGVAVQHA VLKIIDELEI KTLGSGEKSG SGGAPTPIGM YALREYLSAR STVEDKLLGS V DAESGKTK ...String:
KRAALIQNLR DSYTETSSFA VIEEWAAGTL QEIEGIAKAA AEAHGVIRNS TYGRAQAEKS PEQLLGVLQR YQDLCHNVYC QAETIRTVI AIRIPEHKEA DNLGVAVQHA VLKIIDELEI KTLGSGEKSG SGGAPTPIGM YALREYLSAR STVEDKLLGS V DAESGKTK GGSQSPSLLL ELRQIDADFM LKVELATTHL STMVRAVINA YLLNWKKLIQ PRTGNLSYYT

UniProtKB: Proteasome activator protein PA26

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration20 mg/mL
BufferpH: 7.6
Component:
ConcentrationNameFormula
20.0 mMHEPES
25.0 mMsodium chlorideNaCl
25.0 mMpotassium chlorideKCl
1.0 mMTCEP
0.05 % (w/v)Nonidet P-40
GridModel: Quantifoil R2/2 / Material: COPPER / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 277 K / Instrument: HOMEMADE PLUNGER
Details: Specimens were manually blotted with Whatman #1 filter paper..

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
DetailsImages were acquired in nanoprobe mode.
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 3710 pixel / Digitization - Dimensions - Height: 3838 pixel / Digitization - Frames/image: 1-25 / Number grids imaged: 1 / Number real images: 11656 / Average exposure time: 6.25 sec. / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Calibrated defocus max: -3.0 µm / Calibrated defocus min: -1.5 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: -2.5 µm / Nominal defocus min: -1.0 µm / Nominal magnification: 29000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

DetailsCamera was operated in counting mode.
Particle selectionNumber selected: 579361
Details: Particles were selected using the Relion template-based particle picker.
Startup model#0 - Type of model: PDB ENTRY
#0 - PDB model - PDB ID:

1yau


#0 - Details: PA26 activator / #1 - Type of model: PDB ENTRY
#1 - PDB model - PDB ID:

5a0q


#1 - Details: human 20S proteasome
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 2.1) / Number images used: 234960
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 2.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 2.1)
FSC plot (resolution estimation)

-
Atomic model buiding 1

RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-6xmj:
Human 20S proteasome bound to an engineered 11S (PA26) activator

+
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://pdbjlvh1.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