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- EMDB-31728: 20S proteasome incubated with monoUb-CyclinB1-NT (S0) -

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Basic information

Entry
Database: EMDB / ID: EMD-31728
Title20S proteasome incubated with monoUb-CyclinB1-NT (S0)
Map data
Sample
  • Complex: 20S proteasome incubated with monoUb CyclinB1-NT
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.38 Å
AuthorsXu C / Cong Y
Funding support Israel, 1 items
OrganizationGrant numberCountry
Israel Science Foundation Israel
CitationJournal: Nat Commun / Year: 2021
Title: The 20S as a stand-alone proteasome in cells can degrade the ubiquitin tag.
Authors: Indrajit Sahu / Sachitanand M Mali / Prasad Sulkshane / Cong Xu / Andrey Rozenberg / Roni Morag / Manisha Priyadarsini Sahoo / Sumeet K Singh / Zhanyu Ding / Yifan Wang / Sharleen Day / Yao ...Authors: Indrajit Sahu / Sachitanand M Mali / Prasad Sulkshane / Cong Xu / Andrey Rozenberg / Roni Morag / Manisha Priyadarsini Sahoo / Sumeet K Singh / Zhanyu Ding / Yifan Wang / Sharleen Day / Yao Cong / Oded Kleifeld / Ashraf Brik / Michael H Glickman /
Abstract: The proteasome, the primary protease for ubiquitin-dependent proteolysis in eukaryotes, is usually found as a mixture of 30S, 26S, and 20S complexes. These complexes have common catalytic sites, ...The proteasome, the primary protease for ubiquitin-dependent proteolysis in eukaryotes, is usually found as a mixture of 30S, 26S, and 20S complexes. These complexes have common catalytic sites, which makes it challenging to determine their distinctive roles in intracellular proteolysis. Here, we chemically synthesize a panel of homogenous ubiquitinated proteins, and use them to compare 20S and 26S proteasomes with respect to substrate selection and peptide-product generation. We show that 20S proteasomes can degrade the ubiquitin tag along with the conjugated substrate. Ubiquitin remnants on branched peptide products identified by LC-MS/MS, and flexibility in the 20S gate observed by cryo-EM, reflect the ability of the 20S proteasome to proteolyze an isopeptide-linked ubiquitin-conjugate. Peptidomics identifies proteasome-trapped ubiquitin-derived peptides and peptides of potential 20S substrates in Hi20S cells, hypoxic cells, and human failing-heart. Moreover, elevated levels of 20S proteasomes appear to contribute to cell survival under stress associated with damaged proteins.
History
DepositionAug 17, 2021-
Header (metadata) releaseSep 22, 2021-
Map releaseSep 22, 2021-
UpdateMar 30, 2022-
Current statusMar 30, 2022Processing site: PDBj / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.03
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.03
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_31728.png

Downloads & links

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Map

FileDownload / File: emd_31728.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.318 Å
Density
Contour LevelBy AUTHOR: 0.03 / Movie #1: 0.03
Minimum - Maximum-0.093531765 - 0.15690984
Average (Standard dev.)-0.00012427599 (±0.008856142)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions200200200
Spacing200200200
CellA=B=C: 263.6 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.3181.3181.318
M x/y/z200200200
origin x/y/z0.0000.0000.000
length x/y/z263.600263.600263.600
α/β/γ90.00090.00090.000
start NX/NY/NZ-64-64-64
NX/NY/NZ128128128
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS200200200
D min/max/mean-0.0940.157-0.000

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Supplemental data

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Sample components

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Entire : 20S proteasome incubated with monoUb CyclinB1-NT

EntireName: 20S proteasome incubated with monoUb CyclinB1-NT
Components
  • Complex: 20S proteasome incubated with monoUb CyclinB1-NT

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Supramolecule #1: 20S proteasome incubated with monoUb CyclinB1-NT

SupramoleculeName: 20S proteasome incubated with monoUb CyclinB1-NT / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#14
Source (natural)Organism: Homo sapiens (human)

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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: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 38.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.38 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 282834
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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