5YZG
The Cryo-EM Structure of Human Catalytic Step I Spliceosome (C complex) at 4.1 angstrom resolution
This is a non-PDB format compatible entry.
Summary for 5YZG
| Entry DOI | 10.2210/pdb5yzg/pdb |
| EMDB information | 6721 6864 |
| Descriptor | Pre-mRNA-processing-splicing factor 8, Crooked neck-like protein 1, Pre-mRNA-splicing factor SPF27, ... (51 entities in total) |
| Functional Keywords | structure of a human catalytic step i spliceosome, splicing |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 55 |
| Total formula weight | 3193815.30 |
| Authors | |
| Primary citation | Zhan, X.,Yan, C.,Zhang, X.,Lei, J.,Shi, Y. Structure of a human catalytic step I spliceosome Science, 359:537-545, 2018 Cited by PubMed Abstract: Splicing by the spliceosome involves branching and exon ligation. The branching reaction leads to the formation of the catalytic step I spliceosome (C complex). Here we report the cryo-electron microscopy structure of the human C complex at an average resolution of 4.1 angstroms. Compared with the C complex, the human complex contains 11 additional proteins. The step I splicing factors CCDC49 and CCDC94 (Cwc25 and Yju2 in , respectively) closely interact with the DEAH-family adenosine triphosphatase/helicase Prp16 and bridge the gap between Prp16 and the active-site RNA elements. These features, together with structural comparison of the human C and C* complexes, provide mechanistic insights into ribonucleoprotein remodeling and allow the proposition of a working mechanism for the C-to-C* transition. PubMed: 29301961DOI: 10.1126/science.aar6401 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.1 Å) |
Structure validation
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