8IJU
ATP-dependent RNA helicase DDX39A (URH49delta41)
Summary for 8IJU
| Entry DOI | 10.2210/pdb8iju/pdb |
| Descriptor | ATP-dependent RNA helicase DDX39A, TRIETHYLENE GLYCOL, PHOSPHATE ION, ... (5 entities in total) |
| Functional Keywords | atp-dependent rna helicase, rna binding protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 46965.99 |
| Authors | |
| Primary citation | Fujita, K.I.,Ito, M.,Irie, M.,Harada, K.,Fujiwara, N.,Ikeda, Y.,Yoshioka, H.,Yamazaki, T.,Kojima, M.,Mikami, B.,Mayeda, A.,Masuda, S. Structural differences between the closely related RNA helicases, UAP56 and URH49, fashion distinct functional apo-complexes. Nat Commun, 15:455-455, 2024 Cited by PubMed Abstract: mRNA export is an essential pathway for the regulation of gene expression. In humans, closely related RNA helicases, UAP56 and URH49, shape selective mRNA export pathways through the formation of distinct complexes, known as apo-TREX and apo-AREX complexes, and their subsequent remodeling into similar ATP-bound complexes. Therefore, defining the unidentified components of the apo-AREX complex and elucidating the molecular mechanisms underlying the formation of distinct apo-complexes is key to understanding their functional divergence. In this study, we identify additional apo-AREX components physically and functionally associated with URH49. Furthermore, by comparing the structures of UAP56 and URH49 and performing an integrated analysis of their chimeric mutants, we exhibit unique structural features that would contribute to the formation of their respective complexes. This study provides insights into the specific structural and functional diversification of these two helicases that diverged from the common ancestral gene Sub2. PubMed: 38225262DOI: 10.1038/s41467-023-44217-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.82 Å) |
Structure validation
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