9L5Y

Structure of Ro60 dimer from Thermus phage phiLo

9L5Y の概要

• エントリーDOI: 10.2210/pdb9l5y/pdb
• 関連するPDBエントリー: 9KOP
• EMDBエントリー: 62848
• 分子名称: TROVE domain-containing protein, RNA (62-MER) (2 entities in total)
• 機能のキーワード: ro60, trove, rsr, y-rna, cryo-em, protein-rna complex, rna binding protein/rna, rna binding protein-rna complex
• 由来する生物種: Thermus phage phiLo; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 154269.60

構造登録者

Hu, Z.,Huang, Y. (登録日: 2024-12-23, 公開日: 2025-12-10)

主引用文献

Hu, Z.,Jin, Z.,Guo, L.,Zeng, L.,Dong, X.,Jiang, L.,Dai, W.,Ma, J.,Huang, Y.
Structural and molecular mechanisms of an Ro60 homolog from a Thermus bacteriophage.
Nucleic Acids Res., 53:-, 2025

PubMed Abstract: Ro60 is a conserved RNA-binding protein essential for RNA quality control and implicated in autoimmune responses. In this study, we present the structural and functional characterization of φRo60, an Ro60 homolog from Thermus phage phiLo, with its crystal structure determined at 1.99 Å. Despite limited sequence identity with bacterial and amphibian homologs, φRo60 maintains the canonical doughnut-shaped architecture comprising HEAT repeats and a von Willebrand factor A domain. Surface electrostatic analysis reveals an extensive positively charged region across multiple α-helices, likely facilitating diverse RNA interactions. Moreover, φRo60 binds two Y RNA-like molecules (Yrl1 and Yrl2), identified from the phiLo genome, with distinct stoichiometries, leading to the formation of higher-order nucleocytoplasmic ribonucleoprotein (RNP) complexes. Cryo-electron microscopy of φRo60-Yrl2 RNP complexes revealed a minor population adopting a dimeric assembly, and key positively charged residues are important for φRo60-Yrl2 interactions. Additionally, φRo60 and Yrls interact with host Thermus thermophilus HB8 polynucleotide phosphorylase (PNPase), forming tripartite RYPER-like complexes and attenuating the ribonuclease activity of PNPase. These findings highlight φRo60 as a structurally adaptable Ro60 homolog capable of diverse RNA interactions and host factor recruitment, implying unique strategies for phages to counteract host defense systems in thermophilic environments.

PubMed: 40464688
DOI: 10.1093/nar/gkaf470

実験手法

ELECTRON MICROSCOPY (3.81 Å)