3HD4
MHV Nucleocapsid Protein NTD
Summary for 3HD4
| Entry DOI | 10.2210/pdb3hd4/pdb |
| Descriptor | Nucleoprotein (2 entities in total) |
| Functional Keywords | beta platform beta hairpin, golgi apparatus, nucleus, phosphoprotein, ribonucleoprotein, rna-binding, transcription, transcription regulation, viral nucleoprotein, virion, viral protein |
| Biological source | Murine hepatitis virus (MHV-A59) |
| Cellular location | Virion (By similarity): P03416 |
| Total number of polymer chains | 1 |
| Total formula weight | 15542.07 |
| Authors | Giedroc, D.P.,Keane, S.C.,Dann III, C.E. (deposition date: 2009-05-06, release date: 2009-11-17, Last modification date: 2024-02-21) |
| Primary citation | 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 Cited by 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: 19782089DOI: 10.1016/j.jmb.2009.09.040 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.747 Å) |
Structure validation
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