6J6N

Cryo-EM structure of the yeast B*-b1 complex at an average resolution of 3.86 angstrom

6J6N の概要

• エントリーDOI: 10.2210/pdb6j6n/pdb
• EMDBエントリー: 0691
• 分子名称: Pre-mRNA-splicing factor 8, Pre-mRNA-splicing factor CWC22, Pre-mRNA-splicing factor CEF1, ... (35 entities in total)
• 機能のキーワード: spliceosme, b* complex, branching, snrnp, u snrna, splicing
• 由来する生物種: Saccharomyces cerevisiae S288c (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 41
• 化学式量合計: 2075792.28

構造登録者

Wan, R.,Bai, R.,Yan, C.,Lei, J.,Shi, Y. (登録日: 2019-01-15, 公開日: 2019-04-24, 最終更新日: 2020-10-14)

主引用文献

Wan, R.,Bai, R.,Yan, C.,Lei, J.,Shi, Y.
Structures of the Catalytically Activated Yeast Spliceosome Reveal the Mechanism of Branching.
Cell, 177:339-351.e13, 2019

PubMed Abstract: Pre-mRNA splicing is executed by the spliceosome. Structural characterization of the catalytically activated complex (B) is pivotal for understanding the branching reaction. In this study, we assembled the B complexes on two different pre-mRNAs from Saccharomyces cerevisiae and determined the cryo-EM structures of four distinct B complexes at overall resolutions of 2.9-3.8 Å. The duplex between U2 small nuclear RNA (snRNA) and the branch point sequence (BPS) is discretely away from the 5'-splice site (5'SS) in the three B complexes that are devoid of the step I splicing factors Yju2 and Cwc25. Recruitment of Yju2 into the active site brings the U2/BPS duplex into the vicinity of 5'SS, with the BPS nucleophile positioned 4 Å away from the catalytic metal M2. This analysis reveals the functional mechanism of Yju2 and Cwc25 in branching. These structures on different pre-mRNAs reveal substrate-specific conformations of the spliceosome in a major functional state.

PubMed: 30879786
DOI: 10.1016/j.cell.2019.02.006

実験手法

ELECTRON MICROSCOPY (3.86 Å)