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- PDB-9d4u: Core particle assembly intermediate Capless 13S purified from Sac... -
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Open data
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Basic information
Entry | Database: PDB / ID: 9d4u | ||||||||||||||||||||||||||||||
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Title | Core particle assembly intermediate Capless 13S purified from Saccharomyces cerevisiae | ||||||||||||||||||||||||||||||
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![]() | HYDROLASE / Proteasome / Cryo-EM / Assembly / assembly chaperone / Blm10 / PA200 / Blm10-13S / Pba1 / CP | ||||||||||||||||||||||||||||||
Function / homology | ![]() proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / proteasomal ubiquitin-independent protein catabolic process / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / Regulation of PTEN stability and activity / CDK-mediated phosphorylation and removal of Cdc6 / 3-deoxy-7-phosphoheptulonate synthase ...proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / proteasomal ubiquitin-independent protein catabolic process / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / Regulation of PTEN stability and activity / CDK-mediated phosphorylation and removal of Cdc6 / 3-deoxy-7-phosphoheptulonate synthase / 3-deoxy-7-phosphoheptulonate synthase activity / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / KEAP1-NFE2L2 pathway / Neddylation / Orc1 removal from chromatin / MAPK6/MAPK4 signaling / proteasome storage granule / Antigen processing: Ubiquitination & Proteasome degradation / chorismate biosynthetic process / Ub-specific processing proteases / proteasome endopeptidase complex / endopeptidase activator activity / proteasome core complex, beta-subunit complex / proteasome assembly / aromatic amino acid family biosynthetic process / threonine-type endopeptidase activity / proteasome core complex, alpha-subunit complex / amino acid biosynthetic process / Neutrophil degranulation / proteasome complex / ubiquitin-dependent protein catabolic process / endopeptidase activity / proteasome-mediated ubiquitin-dependent protein catabolic process / DNA damage response / endoplasmic reticulum membrane / mitochondrion / metal ion binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||||||||||||||||||||||||||
Biological species | ![]() ![]() | ||||||||||||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.55 Å | ||||||||||||||||||||||||||||||
![]() | Chen, X. / Kaur, M. / Roelofs, J. / Walters, K.J. | ||||||||||||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of Blm10:13S proteasome assembly intermediate reveals parallel assembly pathways for the proteasome core particle Authors: Kaur, M. / Chen, X. / Lee, S.Y. / Weaver, T.M. / Freudenthal, B.D. / Walters, K.J. / Roelofs, J. | ||||||||||||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 792.7 KB | Display | ![]() |
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PDB format | ![]() | 664.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.2 MB | Display | ![]() |
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Full document | ![]() | 1.2 MB | Display | |
Data in XML | ![]() | 70.8 KB | Display | |
Data in CIF | ![]() | 109.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 46570MC ![]() 9d35C ![]() 9d3iC ![]() 9d4cC C: citing same article ( M: map data used to model this data |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
-Proteasome subunit alpha type- ... , 6 types, 6 molecules ABCDEF
#1: Protein | Mass: 28033.830 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: SCL1, PRC2, PRS2, YGL011C / Production host: ![]() ![]() |
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#2: Protein | Mass: 27191.828 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: PRE8, PRS4, YML092C / Production host: ![]() ![]() |
#3: Protein | Mass: 28748.230 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: PRE9, PRS5, YGR135W / Production host: ![]() ![]() |
#4: Protein | Mass: 28478.111 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: PRE6, YOL038W / Production host: ![]() ![]() |
#5: Protein | Mass: 28649.086 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: PUP2, DOA5, YGR253C, G9155 / Production host: ![]() ![]() |
#6: Protein | Mass: 25634.000 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: PRE5, YMR314W, YM9924.06 / Production host: ![]() ![]() |
-Protein , 2 types, 2 molecules GP
#7: Protein | Mass: 31575.068 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: PRE10, PRC1, PRS1, YOR362C, O6650 / Production host: ![]() ![]() |
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#11: Protein | Mass: 22753.646 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: UMP1, YBR173C, YBR1234 / Production host: ![]() ![]() |
-Proteasome subunit beta type- ... , 3 types, 3 molecules IJK
#8: Protein | Mass: 28299.889 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: PUP1, YOR157C / Production host: ![]() ![]() References: UniProt: P25043, proteasome endopeptidase complex |
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#9: Protein | Mass: 22627.842 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: PUP3, YER094C / Production host: ![]() ![]() |
#10: Protein | Mass: 22545.676 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: PRE1, YER012W / Production host: ![]() ![]() |
-Details
Has protein modification | N |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: Proteasome assembly intermediate / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT | |||||||||||||||||||||||||
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Molecular weight | Value: 0.288 MDa / Experimental value: NO | |||||||||||||||||||||||||
Source (natural) | Organism: ![]() ![]() | |||||||||||||||||||||||||
Source (recombinant) | Organism: ![]() ![]() | |||||||||||||||||||||||||
Buffer solution | pH: 7.5 | |||||||||||||||||||||||||
Buffer component |
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Specimen | Conc.: 1.8 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | |||||||||||||||||||||||||
Specimen support | Details: 0.42 mBar, 15mA / Grid material: COPPER / Grid mesh size: 400 divisions/in. / Grid type: Quantifoil R1.2/1.3 | |||||||||||||||||||||||||
Vitrification | Instrument: LEICA EM GP / Cryogen name: ETHANE / Humidity: 80 % / Chamber temperature: 298.15 K |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: TFS KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 81000 X / Nominal defocus max: 2500 nm / Nominal defocus min: 900 nm / Cs: 2.7 mm |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Num. of real images: 5235 |
EM imaging optics | Energyfilter name: GIF Bioquantum |
Image scans | Width: 5760 / Height: 4092 |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 4058518 | ||||||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 3.55 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 108417 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||
Atomic model building | B value: 128.66 / Protocol: RIGID BODY FIT / Space: REAL / Target criteria: Cross-correlation coefficient | ||||||||||||||||||||||||||||||||||||
Atomic model building | 3D fitting-ID: 1 / Accession code: 7LSX / Initial refinement model-ID: 1 / PDB-ID: 7LSX / Source name: PDB / Type: experimental model
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Refinement | Highest resolution: 3.55 Å |