2C86

x-ray structure of the N and C-terminal domain of coronavirus nucleocapsid protein.

Summary for 2C86

• Entry DOI: 10.2210/pdb2c86/pdb
• Related: 2BTL 2BXX
• Descriptor: NUCLEOCAPSID PROTEIN (2 entities in total)
• Functional Keywords: nucleocapsid protein, phosphorylation, rna-binding, viral nucleoprotein
• Biological source: AVIAN INFECTIOUS BRONCHITIS VIRUS
• Cellular location: Virion (By similarity): P69598
• Total number of polymer chains: 2
• Total formula weight: 30029.10

Authors

Jayaram, H.,Fan, H.,Bowman, B.R.,Ooi, A.,Jayaram, J.,Collinson, E.W.,Lescar, J.,Prasad, B.V.V. (deposition date: 2005-12-02, release date: 2006-06-21, Last modification date: 2023-12-13)

Primary citation

Jayaram, H.,Fan, H.,Bowman, B.R.,Ooi, A.,Jayaram, J.,Collisson, E.W.,Lescar, J.,Prasad, B.V.V.
X-Ray Structures of the N- and C-Terminal Domains of a Coronavirus Nucleocapsid Protein: Implications for Nucleocapsid Formation.
J.Virol., 80:6612-, 2006

PubMed Abstract: Coronaviruses cause a variety of respiratory and enteric diseases in animals and humans including severe acute respiratory syndrome. In these enveloped viruses, the filamentous nucleocapsid is formed by the association of nucleocapsid (N) protein with single-stranded viral RNA. The N protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. We describe the structure of the two proteolytically resistant domains of the N protein from infectious bronchitis virus (IBV), a prototype coronavirus. These domains are located at its N- and C-terminal ends (NTD and CTD, respectively). The NTD of the IBV Gray strain at 1.3-A resolution exhibits a U-shaped structure, with two arms rich in basic residues, providing a module for specific interaction with RNA. The CTD forms a tightly intertwined dimer with an intermolecular four-stranded central beta-sheet platform flanked by alpha helices, indicating that the basic building block for coronavirus nucleocapsid formation is a dimeric assembly of N protein. The variety of quaternary arrangements of the NTD and CTD revealed by the analysis of the different crystal forms delineates possible interfaces that could be used for the formation of a flexible filamentous ribonucleocapsid. The striking similarity between the dimeric structure of CTD and the nucleocapsid-forming domain of a distantly related arterivirus indicates a conserved mechanism of nucleocapsid formation for these two viral families.

PubMed: 16775348
DOI: 10.1128/JVI.00157-06

Experimental method

X-RAY DIFFRACTION (3 Å)