7Q4P

U2 snRNP after ATP-dependent remodelling

7Q4P の概要

• エントリーDOI: 10.2210/pdb7q4p/pdb
• 関連するPDBエントリー: 7Q3L 7Q4O
• EMDBエントリー: 13812
• 分子名称: Splicing factor 3A subunit 2, U2 snRNA, Splicing factor 3A subunit 3, ... (10 entities in total)
• 機能のキーワード: snrnp, spliceosome, u2 snrnp, splicing, nuclear protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 573558.33

構造登録者

Tholen, J.,Galej, W.P. (登録日: 2021-11-01, 公開日: 2022-03-30, 最終更新日: 2024-07-17)

主引用文献

Tholen, J.,Razew, M.,Weis, F.,Galej, W.P.
Structural basis of branch site recognition by the human spliceosome.
Science, 375:50-57, 2022

PubMed Abstract: Recognition of the intron branch site (BS) by the U2 small nuclear ribonucleoprotein (snRNP) is a critical event during spliceosome assembly. In mammals, BS sequences are poorly conserved, and unambiguous intron recognition cannot be achieved solely through a base-pairing mechanism. We isolated human 17 U2 snRNP and reconstituted in vitro its adenosine 5´-triphosphate (ATP)–dependent remodeling and binding to the pre–messenger RNA substrate. We determined a series of high-resolution (2.0 to 2.2 angstrom) structures providing snapshots of the BS selection process. The substrate-bound U2 snRNP shows that SF3B6 stabilizes the BS:U2 snRNA duplex, which could aid binding of introns with poor sequence complementarity. ATP-dependent remodeling uncoupled from substrate binding captures U2 snRNA in a conformation that competes with BS recognition, providing a selection mechanism based on branch helix stability.

PubMed: 34822310
DOI: 10.1126/science.abm4245

実験手法

ELECTRON MICROSCOPY (2.15 Å)