5LQW
yeast activated spliceosome
Summary for 5LQW
| Entry DOI | 10.2210/pdb5lqw/pdb |
| EMDB information | 4099 |
| Descriptor | Pre-mRNA-splicing factor 8, Pre-mRNA-splicing factor CWC26, Pre-mRNA-processing protein 45, ... (31 entities in total) |
| Functional Keywords | activated spliceosome, spliceosome, pre-mrna splicing, splicing |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Total number of polymer chains | 31 |
| Total formula weight | 2351190.07 |
| Authors | Rauhut, R.,Luehrmann, R. (deposition date: 2016-08-17, release date: 2016-10-05, Last modification date: 2024-05-08) |
| Primary citation | Rauhut, R.,Fabrizio, P.,Dybkov, O.,Hartmuth, K.,Pena, V.,Chari, A.,Kumar, V.,Lee, C.T.,Urlaub, H.,Kastner, B.,Stark, H.,Luehrmann, R. Molecular architecture of the Saccharomyces cerevisiae activated spliceosome Science, 6306:1399-1405, 2016 Cited by PubMed Abstract: The activated spliceosome (B) is in a catalytically inactive state and is remodeled into a catalytically active machine by the RNA helicase Prp2, but the mechanism is unclear. Here, we describe a 3D electron cryomicroscopy structure of the Saccharomyces cerevisiae B complex at 5.8-angstrom resolution. Our model reveals that in B, the catalytic U2/U6 RNA-Prp8 ribonucleoprotein core is already established, and the 5' splice site (ss) is oriented for step 1 catalysis but occluded by protein. The first-step nucleophile-the branchsite adenosine-is sequestered within the Hsh155 HEAT domain and is held 50 angstroms away from the 5'ss. Our structure suggests that Prp2 adenosine triphosphatase-mediated remodeling leads to conformational changes in Hsh155's HEAT domain that liberate the first-step reactants for catalysis. PubMed: 27562955DOI: 10.1126/science.aag1906 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (5.8 Å) |
Structure validation
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