3HD4

MHV Nucleocapsid Protein NTD

3HD4 の概要

• エントリーDOI: 10.2210/pdb3hd4/pdb
• 分子名称: Nucleoprotein (2 entities in total)
• 機能のキーワード: beta platform beta hairpin, golgi apparatus, nucleus, phosphoprotein, ribonucleoprotein, rna-binding, transcription, transcription regulation, viral nucleoprotein, virion, viral protein
• 由来する生物種: Murine hepatitis virus (MHV-A59)
• 細胞内の位置: Virion (By similarity): P03416
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15542.07

構造登録者

Giedroc, D.P.,Keane, S.C.,Dann III, C.E. (登録日: 2009-05-06, 公開日: 2009-11-17, 最終更新日: 2024-02-21)

主引用文献

Grossoehme, N.E.,Li, L.,Keane, S.C.,Liu, P.,Dann III, C.E.,Leibowitz, J.L.,Giedroc, D.P.
Coronavirus N Protein N-Terminal Domain (NTD) Specifically Binds the Transcriptional Regulatory Sequence (TRS) and Melts TRS-cTRS RNA Duplexes.
J.Mol.Biol., 394:544-557, 2009

PubMed Abstract: All coronaviruses (CoVs), including the causative agent of severe acute respiratory syndrome (SARS), encode a nucleocapsid (N) protein that harbors two independent RNA binding domains of known structure, but poorly characterized RNA binding properties. We show here that the N-terminal domain (NTD) of N protein from mouse hepatitis virus (MHV), a virus most closely related to SARS-CoV, employs aromatic amino acid-nucleobase stacking interactions with a triple adenosine motif to mediate high-affinity binding to single-stranded RNAs containing the transcriptional regulatory sequence (TRS) or its complement (cTRS). Stoichiometric NTD fully unwinds a TRS-cTRS duplex that mimics a transiently formed transcription intermediate in viral subgenomic RNA synthesis. Mutation of the solvent-exposed Y127, positioned on the beta-platform surface of our 1.75 A structure, binds the TRS far less tightly and is severely crippled in its RNA unwinding activity. In contrast, the C-terminal domain (CTD) exhibits no RNA unwinding activity. Viruses harboring Y127A N mutation are strongly selected against and Y127A N does not support an accessory function in MHV replication. We propose that the helix melting activity of the coronavirus N protein NTD plays a critical accessory role in subgenomic RNA synthesis and other processes requiring RNA remodeling.

PubMed: 19782089
DOI: 10.1016/j.jmb.2009.09.040

実験手法

X-RAY DIFFRACTION (1.747 Å)