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- EMDB-17798: CUL2-RBX1-ELOB/C-FEM1C-SIL1 conformation 1 -

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Basic information

Entry
Database: EMDB / ID: EMD-17798
TitleCUL2-RBX1-ELOB/C-FEM1C-SIL1 conformation 1
Map dataDeepEMhancer sharpened map
Sample
  • Complex: CUL2-RBX1-ELOB/C-FEM1C-SIL1 conformation 1
KeywordsCUL2 / FEM1C / ELOB/C / SIL1 / Ubiquitin / Ubiquitin Ligase / LIGASE
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 7.72 Å
AuthorsLiwocha J / Prabu JR / Kleiger G / Schulman BA
Funding support Germany, 1 items
OrganizationGrant numberCountry
Max Planck Society Germany
CitationJournal: Nat Struct Mol Biol / Year: 2024
Title: Mechanism of millisecond Lys48-linked poly-ubiquitin chain formation by cullin-RING ligases.
Authors: Joanna Liwocha / Jerry Li / Nicholas Purser / Chutima Rattanasopa / Samuel Maiwald / David T Krist / Daniel C Scott / Barbara Steigenberger / J Rajan Prabu / Brenda A Schulman / Gary Kleiger /
Abstract: E3 ubiquitin ligases, in collaboration with E2 ubiquitin-conjugating enzymes, modify proteins with poly-ubiquitin chains. Cullin-RING ligase (CRL) E3s use Cdc34/UBE2R-family E2s to build Lys48-linked ...E3 ubiquitin ligases, in collaboration with E2 ubiquitin-conjugating enzymes, modify proteins with poly-ubiquitin chains. Cullin-RING ligase (CRL) E3s use Cdc34/UBE2R-family E2s to build Lys48-linked poly-ubiquitin chains to control an enormous swath of eukaryotic biology. Yet the molecular mechanisms underlying this exceptional linkage specificity and millisecond kinetics of poly-ubiquitylation remain unclear. Here we obtain cryogenic-electron microscopy (cryo-EM) structures that provide pertinent insight into how such poly-ubiquitin chains are forged. The CRL RING domain not only activates the E2-bound ubiquitin but also shapes the conformation of a distinctive UBE2R2 loop, positioning both the ubiquitin to be transferred and the substrate-linked acceptor ubiquitin within the active site. The structures also reveal how the ubiquitin-like protein NEDD8 uniquely activates CRLs during chain formation. NEDD8 releases the RING domain from the CRL, but unlike previous CRL-E2 structures, does not contact UBE2R2. These findings suggest how poly-ubiquitylation may be accomplished by many E2s and E3s.
History
DepositionJul 7, 2023-
Header (metadata) releaseFeb 14, 2024-
Map releaseFeb 14, 2024-
UpdateFeb 28, 2024-
Current statusFeb 28, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_17798.png

Downloads & links

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Map

FileDownload / File: emd_17798.map.gz / Format: CCP4 / Size: 18.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationDeepEMhancer sharpened map
Projections & slices

Image control

Size
Brightness
Contrast
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

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.885 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0487
Minimum - Maximum-0.0017457181 - 1.8010544
Average (Standard dev.)0.0011617901 (±0.023792198)
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_17798_msk_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

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Additional map: Relion PostProcessed Map

Fileemd_17798_additional_1.map
AnnotationRelion PostProcessed Map
Projections & Slices
AxesZYX

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Half map: #2

Fileemd_17798_half_map_1.map
Projections & Slices
AxesZYX

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Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_17798_half_map_2.map
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

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Sample components

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Entire : CUL2-RBX1-ELOB/C-FEM1C-SIL1 conformation 1

EntireName: CUL2-RBX1-ELOB/C-FEM1C-SIL1 conformation 1
Components
  • Complex: CUL2-RBX1-ELOB/C-FEM1C-SIL1 conformation 1

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Supramolecule #1: CUL2-RBX1-ELOB/C-FEM1C-SIL1 conformation 1

SupramoleculeName: CUL2-RBX1-ELOB/C-FEM1C-SIL1 conformation 1 / type: complex / ID: 1 / Parent: 0
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 190 KDa

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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: 0.6 µm

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Image processing

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

5n4w

Final reconstructionResolution.type: BY AUTHOR / Resolution: 7.72 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 56038
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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