Summary for 6N7X
| Entry DOI | 10.2210/pdb6n7x/pdb |
| EMDB information | 8622 |
| Descriptor | U1 small nuclear ribonucleoprotein 70 kDa homolog, Small nuclear ribonucleoprotein Sm D1, Small nuclear ribonucleoprotein Sm D2, ... (16 entities in total) |
| Functional Keywords | pre-mrna splicing, u1 snrnp, alternative splicing, rna binding protein-rna complex, rna binding protein/rna |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 16 |
| Total formula weight | 694678.06 |
| Authors | Li, X.,Liu, S.,Jiang, J.,Zhang, L.,Espinosa, S.,Hill, R.C.,Hansen, K.C.,Zhou, Z.H.,Zhao, R. (deposition date: 2018-11-28, release date: 2019-07-24, Last modification date: 2024-03-13) |
| Primary citation | Li, X.,Liu, S.,Jiang, J.,Zhang, L.,Espinosa, S.,Hill, R.C.,Hansen, K.C.,Zhou, Z.H.,Zhao, R. CryoEM structure of Saccharomyces cerevisiae U1 snRNP offers insight into alternative splicing. Nat Commun, 8:1035-1035, 2017 Cited by PubMed Abstract: U1 snRNP plays a critical role in 5'-splice site recognition and is a frequent target of alternative splicing factors. These factors transiently associate with human U1 snRNP and are not amenable for structural studies, while their Saccharomyces cerevisiae (yeast) homologs are stable components of U1 snRNP. Here, we report the cryoEM structure of yeast U1 snRNP at 3.6 Å resolution with atomic models for ten core proteins, nearly all essential domains of its RNA, and five stably associated auxiliary proteins. The foot-shaped yeast U1 snRNP contains a core in the "ball-and-toes" region architecturally similar to the human U1 snRNP. All auxiliary proteins are in the "arch-and-heel" region and connected to the core through the Prp42/Prp39 paralogs. Our demonstration that homodimeric human PrpF39 directly interacts with U1C-CTD, mirroring yeast Prp42/Prp39, supports yeast U1 snRNP as a model for understanding how transiently associated auxiliary proteins recruit human U1 snRNP in alternative splicing. PubMed: 29051543DOI: 10.1038/s41467-017-01241-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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