2MY2

Snu17p-Bud13p structure intermediate during RES complex assembly

2MY2 の概要

• エントリーDOI: 10.2210/pdb2my2/pdb
• 関連するPDBエントリー: 2MKC 2MY3
• NMR情報: BMRB: 25442
• 分子名称: U2 snRNP component IST3, Pre-mRNA-splicing factor CWC26 (2 entities in total)
• 機能のキーワード: spliceosome, snu17p, ist3p, pml1p, heterodimer, cooperativity, res, splicing, rrm
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• 細胞内の位置: Cytoplasm: P40565 P46947
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18384.37

構造登録者

Wysoczanski, P.,Becker, S.,Zweckstetter, M. (登録日: 2015-01-19, 公開日: 2015-08-12, 最終更新日: 2024-05-15)

主引用文献

Wysoczanski, P.,Becker, S.,Zweckstetter, M.
Structures of intermediates during RES complex assembly.
Sci Rep, 5:12545-12545, 2015

PubMed Abstract: The action of the spliceosome depends on the stepwise cooperative assembly and disassembly of its components. Very strong cooperativity was observed for the RES (Retention and Splicing) hetero-trimeric complex where the affinity from binary to tertiary interactions changes more than 100-fold and affects RNA binding. The RES complex is involved in splicing regulation and retention of not properly spliced pre-mRNA with its three components--Snu17p, Pml1p and Bud13p--giving rise to the two possible intermediate dimeric complexes Pml1p-Snu17p and Bud13p-Snu17p. Here we determined the three-dimensional structure and dynamics of the Pml1p-Snu17p and Bud13p-Snu17p dimers using liquid state NMR. We demonstrate that localized as well as global changes occur along the RES trimer assembly pathway. The stepwise rigidification of the Snu17p structure following the binding of Pml1p and Bud13p provides a basis for the strong cooperative nature of RES complex assembly.

PubMed: 26212312
DOI: 10.1038/srep12545

実験手法

SOLUTION NMR