3HAY

Crystal structure of a substrate-bound full H/ACA RNP from Pyrococcus furiosus

3HAY の概要

• エントリーDOI: 10.2210/pdb3hay/pdb
• 関連するPDBエントリー: 3HAX
• 分子名称: Probable tRNA pseudouridine synthase B, Small nucleolar rnp gar1-like protein, Ribosome biogenesis protein Nop10, ... (7 entities in total)
• 機能のキーワード: h/aca, guide rna, rna-protein complex, pseudouridine synthase, isomerase, trna processing, ribonucleoprotein, ribosome biogenesis, rrna processing, ribosomal protein, rna-binding, isomerase-biosynthetic protein-rna complex, isomerase/biosynthetic protein/rna
• 由来する生物種: Pyrococcus furiosus; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 100791.68

構造登録者

Ye, K. (登録日: 2009-05-03, 公開日: 2009-06-23, 最終更新日: 2023-11-01)

主引用文献

Duan, J.,Li, L.,Lu, J.,Wang, W.,Ye, K.
Structural mechanism of substrate RNA recruitment in H/ACA RNA-guided pseudouridine synthase.
Mol.Cell, 34:427-439, 2009

PubMed Abstract: H/ACA RNAs form ribonucleoprotein complex (RNP) with proteins Cbf5, Nop10, L7Ae, and Gar1 and guide site-specific conversion of uridine into pseudouridine in cellular RNAs. The crystal structures of H/ACA RNP with substrate bound at the active site cleft reveal that the substrate is recruited through sequence-specific pairing with guide RNA and essential protein contacts. Substrate binding leads to a reorganization of a preset pseudouridylation pocket and an adaptive movement of the PUA domain and the lower stem of the H/ACA RNA. Moreover, a thumb loop flips from the Gar1-bound state in the substrate-free RNP structure to tightly associate with the substrate. Mutagenesis and enzyme kinetics analysis suggest a critical role of Gar1 and the thumb in substrate turnover, particularly in product release. Comparison with tRNA Psi55 synthase TruB reveals the structural conservation and adaptation between an RNA-guided and stand-alone pseudouridine synthase and provides insight into the guide-independent activity of Cbf5.

PubMed: 19481523
DOI: 10.1016/j.molcel.2009.05.005

実験手法

X-RAY DIFFRACTION (4.99 Å)