6N7P
S. cerevisiae spliceosomal E complex (UBC4)
Summary for 6N7P
| Entry DOI | 10.2210/pdb6n7p/pdb |
| EMDB information | 0360 |
| Descriptor | U1 small nuclear ribonucleoprotein 70 kDa homolog, Pre-mRNA-processing protein PRP40, Small nuclear ribonucleoprotein-associated protein B, ... (22 entities in total) |
| Functional Keywords | pre-mrna splicing, spliceosome, e complex, rna binding protein |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 21 |
| Total formula weight | 944222.10 |
| Authors | Liu, S.,Li, X.,Zhou, Z.H.,Zhao, R. (deposition date: 2018-11-27, release date: 2019-09-18, Last modification date: 2024-03-20) |
| Primary citation | Li, X.,Liu, S.,Zhang, L.,Issaian, A.,Hill, R.C.,Espinosa, S.,Shi, S.,Cui, Y.,Kappel, K.,Das, R.,Hansen, K.C.,Zhou, Z.H.,Zhao, R. A unified mechanism for intron and exon definition and back-splicing. Nature, 573:375-380, 2019 Cited by PubMed Abstract: The molecular mechanisms of exon definition and back-splicing are fundamental unanswered questions in pre-mRNA splicing. Here we report cryo-electron microscopy structures of the yeast spliceosomal E complex assembled on introns, providing a view of the earliest event in the splicing cycle that commits pre-mRNAs to splicing. The E complex architecture suggests that the same spliceosome can assemble across an exon, and that it either remodels to span an intron for canonical linear splicing (typically on short exons) or catalyses back-splicing to generate circular RNA (on long exons). The model is supported by our experiments, which show that an E complex assembled on the middle exon of yeast EFM5 or HMRA1 can be chased into circular RNA when the exon is sufficiently long. This simple model unifies intron definition, exon definition, and back-splicing through the same spliceosome in all eukaryotes and should inspire experiments in many other systems to understand the mechanism and regulation of these processes. PubMed: 31485080DOI: 10.1038/s41586-019-1523-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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