9ESI
Structure of a B-state intermediate committed to discard (Bd-II state)
Summary for 9ESI
| Entry DOI | 10.2210/pdb9esi/pdb |
| Related | 9ESH |
| EMDB information | 19941 19942 |
| Descriptor | Stress response protein bis1, Small nuclear ribonucleoprotein Sm D1, Small nuclear ribonucleoprotein Sm D2, ... (45 entities in total) |
| Functional Keywords | helicase, g-patch protein, discard pathway, splicing |
| Biological source | Schizosaccharomyces pombe (fission yeast) More |
| Total number of polymer chains | 43 |
| Total formula weight | 2165647.88 |
| Authors | Soni, K.,Wild, K.,Sinning, I. (deposition date: 2024-03-26, release date: 2024-12-25, Last modification date: 2025-01-29) |
| Primary citation | Soni, K.,Horvath, A.,Dybkov, O.,Schwan, M.,Trakansuebkul, S.,Flemming, D.,Wild, K.,Urlaub, H.,Fischer, T.,Sinning, I. Structures of aberrant spliceosome intermediates on their way to disassembly. Nat.Struct.Mol.Biol., 2025 Cited by PubMed Abstract: Intron removal during pre-mRNA splicing is of extraordinary complexity and its disruption causes a vast number of genetic diseases in humans. While key steps of the canonical spliceosome cycle have been revealed by combined structure-function analyses, structural information on an aberrant spliceosome committed to premature disassembly is not available. Here, we report two cryo-electron microscopy structures of post-B spliceosome intermediates from Schizosaccharomyces pombe primed for disassembly. We identify the DEAH-box helicase-G-patch protein pair (Gih35-Gpl1, homologous to human DHX35-GPATCH1) and show how it maintains catalytic dormancy. In both structures, Gpl1 recognizes a remodeled active site introduced by an overstabilization of the U5 loop I interaction with the 5' exon leading to a single-nucleotide insertion at the 5' splice site. Remodeling is communicated to the spliceosome surface and the Ntr1 complex that mediates disassembly is recruited. Our data pave the way for a targeted analysis of splicing quality control. PubMed: 39833470DOI: 10.1038/s41594-024-01480-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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