7APK
Structure of the human THO - UAP56 complex
Summary for 7APK
| Entry DOI | 10.2210/pdb7apk/pdb |
| EMDB information | 11853 11854 11855 11856 11857 |
| Descriptor | THO complex subunit 1, THO complex subunit 2, THO complex subunit 3, ... (8 entities in total) |
| Functional Keywords | mrna, nucleocytoplasmic transport, r-loop, gene expression, gene regulation |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 30 |
| Total formula weight | 1836843.28 |
| Authors | Hohmann, U.,Puehringer, T.,Plaschka, C. (deposition date: 2020-10-17, release date: 2020-12-16, Last modification date: 2024-05-01) |
| Primary citation | Puhringer, T.,Hohmann, U.,Fin, L.,Pacheco-Fiallos, B.,Schellhaas, U.,Brennecke, J.,Plaschka, C. Structure of the human core transcription-export complex reveals a hub for multivalent interactions. Elife, 9:-, 2020 Cited by PubMed 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 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. PubMed: 33191911DOI: 10.7554/eLife.61503 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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