9DLV
Cryo-EM structure of the human TREX-2.1 complex (LENG8/PCID2/DSS1) bound to DDX39B(UAP56)
This is a non-PDB format compatible entry.
Summary for 9DLV
| Entry DOI | 10.2210/pdb9dlv/pdb |
| EMDB information | 46985 |
| Descriptor | Leukocyte receptor cluster member 8, PCI domain-containing protein 2, 26S proteasome complex subunit SEM1, ... (4 entities in total) |
| Functional Keywords | mrna nuclear export, trex, trex-2, leng8, uap56, ddx39b, rna binding protein, rna binding protein-hydrolase complex, rna binding protein/hydrolase |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 139857.68 |
| Authors | Clarke, B.P.,Xie, Y.,Ren, Y. (deposition date: 2024-09-11, release date: 2025-09-17, Last modification date: 2025-11-12) |
| Primary citation | Clarke, B.P.,Gao, S.,Mei, M.,Xie, D.,Angelos, A.E.,Vazhavilla, A.,Hill, P.S.,Cagatay, T.,Batten, K.,Shay, J.W.,Xie, Y.,Fontoura, B.M.A.,Ren, Y. Structural mechanism of DDX39B regulation by human TREX-2 and a related complex in mRNP remodeling. Nat Commun, 16:5471-5471, 2025 Cited by PubMed Abstract: Nuclear export of mRNAs in the form of messenger ribonucleoprotein particles (mRNPs) is an obligatory step for eukaryotic gene expression. The DEAD-box ATPase DDX39B (also known as UAP56) is a multifunctional regulator of nuclear mRNPs. How DDX39B mediates mRNP assembly and export in a controlled manner remains elusive. Here, we identify a novel complex TREX-2.1 localized in the nucleus that facilitates the release of DDX39B from the mRNP. TREX-2.1 is composed of three subunits, LENG8, PCID2, and DSS1, and shares the latter two subunits with the nuclear pore complex-associated TREX-2 complex. Cryo-EM structures of TREX-2.1/DDX39B and TREX-2/DDX39B identify a conserved trigger loop in the LENG8 and GANP subunit of the respective TREX-2.1 and TREX-2 complex that is critical for DDX39B regulation. RNA sequencing from LENG8 knockdown cells shows that LENG8 influences the nucleocytoplasmic ratio of a subset of mRNAs with high GC content. Together, our findings lead to a mechanistic understanding of the functional cycle of DDX39B and its regulation by TREX-2 and TREX-2.1 in mRNP processing. PubMed: 40595470DOI: 10.1038/s41467-025-60547-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.97 Å) |
Structure validation
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