|Entry||Database: EMDB / ID: EMD-11853|
|Title||Structure of the human THO - UAP56 complex (Map A)|
|Sample||THO - UAP56|
|Biological species||Homo sapiens (human)|
|Method||single particle reconstruction / cryo EM / Resolution: 3.9 Å|
|Authors||Puehringer T / Hohmann U / Plaschka C|
|Citation||Journal: 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 Report||Summary, Full report, XML, About validation report|
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_11853.map.gz / Format: CCP4 / Size: 325 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.34 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Additional map: Map A sharpened (Map sharpening B-factor -172 A%u030A2)
-Entire THO - UAP56
|Entire||Name: THO - UAP56 / Number of components: 1|
-Component #1: protein, THO - UAP56
|Protein||Name: THO - UAP56 / Recombinant expression: No|
|Mass||Theoretical: 1.836 MDa|
|Source||Species: Homo sapiens (human)|
|Source (engineered)||Expression System: Trichoplusia ni (cabbage looper) / Strain: Hi5|
|Specimen||Specimen state: Particle / Method: cryo EM|
|Sample solution||pH: 7.9|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 50 e/Å2 / Illumination mode: OTHER|
|Lens||Imaging mode: OTHER|
|Specimen Holder||Model: OTHER|
|Image acquisition||Number of digital images: 26303|
|Processing||Method: single particle reconstruction / Number of projections: 195098|
|3D reconstruction||Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF|
-Atomic model buiding
|Modeling #1||Refinement space: REAL|
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