4OOG

Crystal structure of yeast RNase III (Rnt1p) complexed with the product of dsRNA processing

4OOG の概要

• エントリーDOI: 10.2210/pdb4oog/pdb
• 関連するPDBエントリー: 2NUG
• 分子名称: Ribonuclease 3, 34-mer RNA, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: rnase:rna complex, ribonuclease iii domain, double-stranded rna-binding domain, endoribonuclease, dsrna-specific rnase, double-stranded rna, hydrolase-rna complex, hydrolase/rna
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 66549.34

構造登録者

Liang, Y.-H.,Ji, X. (登録日: 2014-02-02, 公開日: 2014-04-16, 最終更新日: 2023-09-20)

主引用文献

Liang, Y.H.,Lavoie, M.,Comeau, M.A.,Abou Elela, S.,Ji, X.
Structure of a Eukaryotic RNase III Postcleavage Complex Reveals a Double-Ruler Mechanism for Substrate Selection.
Mol.Cell, 54:431-444, 2014

PubMed Abstract: Ribonuclease III (RNase III) enzymes are a family of double-stranded RNA (dsRNA)-specific endoribonucleases required for RNA maturation and gene regulation. Prokaryotic RNase III enzymes have been well characterized, but how eukaryotic RNase IIIs work is less clear. Here, we describe the structure of the Saccharomyces cerevisiae RNase III (Rnt1p) postcleavage complex and explain why Rnt1p binds to RNA stems capped with an NGNN tetraloop. The structure shows specific interactions between a structural motif located at the end of the Rnt1p dsRNA-binding domain (dsRBD) and the guanine nucleotide in the second position of the loop. Strikingly, structural and biochemical analyses indicate that the dsRBD and N-terminal domains (NTDs) of Rnt1p function as two rulers that measure the distance between the tetraloop and the cleavage site. These findings provide a framework for understanding eukaryotic RNase IIIs.

PubMed: 24703949
DOI: 10.1016/j.molcel.2014.03.006

実験手法

X-RAY DIFFRACTION (2.5 Å)