3NMU

Crystal Structure of substrate-bound halfmer box C/D RNP

3NMU の概要

• エントリーDOI: 10.2210/pdb3nmu/pdb
• 関連するPDBエントリー: 3NVI 3NVK 3NVM
• 分子名称: NOP5/NOP56 related protein, 50S ribosomal protein L7Ae, RNA (34-MER), ... (7 entities in total)
• 機能のキーワード: kink-turn motif, rna assembly motif, transferase-rna complex, transferase/rna
• 由来する生物種: Pyrococcus furiosus; 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 201013.06

構造登録者

Li, H.,Xue, S.,Wang, R. (登録日: 2010-06-22, 公開日: 2011-05-25, 最終更新日: 2023-12-27)

主引用文献

Xue, S.,Wang, R.,Yang, F.,Terns, R.M.,Terns, M.P.,Zhang, X.,Maxwell, E.S.,Li, H.
Structural basis for substrate placement by an archaeal box C/D ribonucleoprotein particle.
Mol.Cell, 39:939-949, 2010

PubMed Abstract: Box C/D small nucleolar and Cajal body ribonucleoprotein particles (sno/scaRNPs) direct site-specific 2'-O-methylation of ribosomal and spliceosomal RNAs and are critical for gene expression. Here we report crystal structures of an archaeal box C/D RNP containing three core proteins (fibrillarin, Nop56/58, and L7Ae) and a half-mer box C/D guide RNA paired with a substrate RNA. The structure reveals a guide-substrate RNA duplex orientation imposed by a composite protein surface and the conserved GAEK motif of Nop56/58. Molecular modeling supports a dual C/D RNP structure that closely mimics that recently visualized by electron microscopy. The substrate-bound dual RNP model predicts an asymmetric protein distribution between the RNP that binds and methylates the substrate RNA. The predicted asymmetric nature of the holoenzyme is consistent with previous biochemical data on RNP assembly and provides a simple solution for accommodating base-pairing between the C/D guide RNA and large ribosomal and spliceosomal substrate RNAs.

PubMed: 20864039
DOI: 10.1016/j.molcel.2010.08.022

実験手法

X-RAY DIFFRACTION (2.729 Å)