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4YHV

Yeast Prp3 C-terminal fragment 325-469

4YHV の概要
エントリーDOI10.2210/pdb4yhv/pdb
関連するPDBエントリー4YHU 4YHV 4YHW
分子名称U4/U6 small nuclear ribonucleoprotein PRP3, ACETIC ACID (3 entities in total)
機能のキーワードspliceosomal protein, duf1115, rna-binding domain, ferredoxin-like fold, rna binding protein
由来する生物種Saccharomyces cerevisiae (Baker's yeast)
細胞内の位置Nucleus: Q03338
タンパク質・核酸の鎖数1
化学式量合計17481.20
構造登録者
Liu, S.,Wahl, M.C. (登録日: 2015-02-27, 公開日: 2015-07-22, 最終更新日: 2024-01-10)
主引用文献Liu, S.,Mozaffari-Jovin, S.,Wollenhaupt, J.,Santos, K.F.,Theuser, M.,Dunin-Horkawicz, S.,Fabrizio, P.,Bujnicki, J.M.,Luhrmann, R.,Wahl, M.C.
A composite double-/single-stranded RNA-binding region in protein Prp3 supports tri-snRNP stability and splicing.
Elife, 4:e07320-e07320, 2015
Cited by
PubMed Abstract: Prp3 is an essential U4/U6 di-snRNP-associated protein whose functions and molecular mechanisms in pre-mRNA splicing are presently poorly understood. We show by structural and biochemical analyses that Prp3 contains a bipartite U4/U6 di-snRNA-binding region comprising an expanded ferredoxin-like fold, which recognizes a 3'-overhang of U6 snRNA, and a preceding peptide, which binds U4/U6 stem II. Phylogenetic analyses revealed that the single-stranded RNA-binding domain is exclusively found in Prp3 orthologs, thus qualifying as a spliceosome-specific RNA interaction module. The composite double-stranded/single-stranded RNA-binding region assembles cooperatively with Snu13 and Prp31 on U4/U6 di-snRNAs and inhibits Brr2-mediated U4/U6 di-snRNA unwinding in vitro. RNP-disrupting mutations in Prp3 lead to U4/U6•U5 tri-snRNP assembly and splicing defects in vivo. Our results reveal how Prp3 acts as an important bridge between U4/U6 and U5 in the tri-snRNP and comparison with a Prp24-U6 snRNA recycling complex suggests how Prp3 may be involved in U4/U6 reassembly after splicing.
PubMed: 26161500
DOI: 10.7554/eLife.07320
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 4yhv
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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