2MKC
Cooperative Structure of the Heterotrimeric pre-mRNA Retention and Splicing Complex
Summary for 2MKC
| Entry DOI | 10.2210/pdb2mkc/pdb |
| NMR Information | BMRB: 19766 |
| Descriptor | U2 snRNP component IST3, Pre-mRNA leakage protein 1, Pre-mRNA-splicing factor CWC26 (3 entities in total) |
| Functional Keywords | spliceosome, snu17p, bud13p, pml1p, heterotrimer, cooperativity, res, splicing, rrm, protein binding, ist3p |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Cellular location | Cytoplasm: P40565 Q07930 P46947 |
| Total number of polymer chains | 3 |
| Total formula weight | 19838.95 |
| Authors | Wysoczanski, P.,Schneider, C.,Xiang, S.,Munari, F.,Trowitzsch, S.,Wahl, M.C.,Luhrmann, R.,Becker, S.,Zweckstetter, M. (deposition date: 2014-02-04, release date: 2014-09-03, Last modification date: 2024-05-15) |
| Primary citation | Wysoczanski, P.,Schneider, C.,Xiang, S.,Munari, F.,Trowitzsch, S.,Wahl, M.C.,Luhrmann, R.,Becker, S.,Zweckstetter, M. Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Nat.Struct.Mol.Biol., 21:911-918, 2014 Cited by PubMed Abstract: The precursor mRNA (pre-mRNA) retention and splicing (RES) complex is a spliceosomal complex that is present in yeast and humans and is important for RNA splicing and retention of unspliced pre-mRNA. Here, we present the solution NMR structure of the RES core complex from Saccharomyces cerevisiae. Complex formation leads to an intricate folding of three components-Snu17p, Bud13p and Pml1p-that stabilizes the RNA-recognition motif (RRM) fold of Snu17p and increases binding affinity in tertiary interactions between the components by more than 100-fold compared to that in binary interactions. RES interacts with pre-mRNA within the spliceosome, and through the assembly of the RES core complex RNA binding efficiency is increased. The three-dimensional structure of the RES core complex highlights the importance of cooperative folding and binding in the functional organization of the spliceosome. PubMed: 25218446DOI: 10.1038/nsmb.2889 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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