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-Structure paper
Title | Structure of a human catalytic step I spliceosome. |
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Journal, issue, pages | Science, Vol. 359, Issue 6375, Page 537-545, Year 2018 |
Publish date | Feb 2, 2018 |
![]() | Xiechao Zhan / Chuangye Yan / Xiaofeng Zhang / Jianlin Lei / Yigong Shi / ![]() |
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 ...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. |
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Methods | EM (single particle) |
Resolution | 4.1 Å |
Structure data | |
Chemicals | ![]() ChemComp-IHP: ![]() ChemComp-GTP: ![]() ChemComp-MG: ![]() ChemComp-ADP: ![]() ChemComp-ZN: ![]() ChemComp-ATP: |
Source |
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![]() | SPLICING / Structure of a Human Catalytic Step I Spliceosome |