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- EMDB-11853: Structure of the human THO - UAP56 complex (Map A) -

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Basic information

Database: EMDB / ID: EMD-11853
TitleStructure of the human THO - UAP56 complex (Map A)
Map data
SampleTHO - UAP56
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.9 Å
AuthorsPuehringer T / Hohmann U / Plaschka C
CitationJournal: Elife / Year: 2020
Title: Structure of the human core transcription-export complex reveals a hub for multivalent interactions.
Authors: Thomas Pühringer / Ulrich Hohmann / Laura Fin / Belén Pacheco-Fiallos / Ulla Schellhaas / Julius Brennecke / Clemens Plaschka /
Abstract: The export of mRNA from nucleus to cytoplasm requires the conserved and essential transcription and export (TREX) complex (THO-UAP56/DDX39B-ALYREF). TREX selectively binds mRNA maturation marks and ...The export of mRNA from nucleus to cytoplasm requires the conserved and essential transcription and export (TREX) complex (THO-UAP56/DDX39B-ALYREF). TREX selectively binds mRNA maturation marks and licenses mRNA for nuclear export by loading the export factor NXF1-NXT1. How TREX integrates these marks and achieves high selectivity for mature mRNA is poorly understood. Here, we report the cryo-electron microscopy structure of the human THO-UAP56/DDX39B complex at 3.3 Å resolution. The seven-subunit THO-UAP56/DDX39B complex multimerizes into a 28-subunit tetrameric assembly, suggesting that selective recognition of mature mRNA is facilitated by the simultaneous sensing of multiple, spatially distant mRNA regions and maturation marks. Two UAP56/DDX39B RNA helicases are juxtaposed at each end of the tetramer, which would allow one bivalent ALYREF protein to bridge adjacent helicases and regulate the TREX-mRNA interaction. Our structural and biochemical results suggest a conserved model for TREX complex function that depends on multivalent interactions between proteins and mRNA.
Validation ReportSummary, Full report, XML, About validation report
DepositionOct 17, 2020-
Header (metadata) releaseDec 16, 2020-
Map releaseDec 16, 2020-
UpdateDec 16, 2020-
Current statusDec 16, 2020Processing site: PDBe / Status: Released

Structure visualization

  • Surface view with section colored by density value
  • Surface level: 0.0288
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.0288
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7apk
  • Surface level: 0.0288
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
Supplemental images

Downloads & links


FileDownload / File: emd_11853.map.gz / Format: CCP4 / Size: 325 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

AxesZ (Sec.)Y (Row.)X (Col.)
1.34 Å/pix.
x 440 pix.
= 589.6 Å
1.34 Å/pix.
x 440 pix.
= 589.6 Å
1.34 Å/pix.
x 440 pix.
= 589.6 Å



Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.34 Å
Contour LevelBy AUTHOR: 0.0288 / Movie #1: 0.0288
Minimum - Maximum-0.030163094 - 0.10694022
Average (Standard dev.)-0.00044098377 (±0.0030647756)
SymmetrySpace group: 1


Map geometry
Axis orderXYZ
CellA=B=C: 589.60004 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.341.341.34
M x/y/z440440440
origin x/y/z0.0000.0000.000
length x/y/z589.600589.600589.600
start NX/NY/NZ1081340
MAP C/R/S123
start NC/NR/NS000
D min/max/mean-0.0300.107-0.000

Supplemental data

Additional map: Map A sharpened (Map sharpening B-factor -172 A%u030A2)

AnnotationMap A sharpened (Map sharpening B-factor -172 A%u030A2)
Projections & Slices


Slices (1/2)
Density Histograms

Sample components

Entire THO - UAP56

EntireName: THO - UAP56 / Number of components: 1

Component #1: protein, THO - UAP56

ProteinName: THO - UAP56 / Recombinant expression: No
MassTheoretical: 1.836 MDa
SourceSpecies: Homo sapiens (human)
Source (engineered)Expression System: Trichoplusia ni (cabbage looper) / Strain: Hi5

Experimental details

Sample preparation

SpecimenSpecimen state: Particle / Method: cryo EM
Sample solutionpH: 7.9
VitrificationCryogen name: ETHANE

Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
ImagingMicroscope: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 50 e/Å2 / Illumination mode: OTHER
LensImaging mode: OTHER
Specimen HolderModel: OTHER
CameraDetector: OTHER

Image acquisition

Image acquisitionNumber of digital images: 26303

Image processing

ProcessingMethod: single particle reconstruction / Number of projections: 195098
3D reconstructionResolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF

Atomic model buiding

Modeling #1Refinement space: REAL

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