2I9F

Structure of the equine arterivirus nucleocapsid protein

Summary for 2I9F

• Entry DOI: 10.2210/pdb2i9f/pdb
• Related: 1P65
• Descriptor: Nucleocapsid, GLYCEROL, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: virus, capsid, assembly, viral protein
• Biological source: Equine arteritis virus
• Total number of polymer chains: 4
• Total formula weight: 31497.27

Authors

Deshpande, A.,Wang, S.,Walsh, M.,Dokland, T. (deposition date: 2006-09-05, release date: 2007-05-01, Last modification date: 2024-10-30)

Primary citation

Deshpande, A.,Wang, S.,Walsh, M.A.,Dokland, T.
Structure of the equine arteritis virus nucleocapsid protein reveals a dimer-dimer arrangement.
Acta Crystallogr.,Sect.D, 63:581-586, 2007

PubMed Abstract: Equine arteritis virus (EAV) is an enveloped positive-sense RNA virus belonging to the Arteriviridae family, which also includes the porcine pathogen PRRSV and is genetically and structurally related to the coronaviruses. EAV is an important equine pathogen that has caused significant economic losses to the horse-breeding industry and has been difficult to control. The EAV virion consists of a genome-containing nucleocapsid core made of nucleocapsid (N) protein surrounded by a lipid envelope containing several membrane proteins. Here, the crystal structure of the capsid-forming domain of the EAV N protein is presented at 2.0 A resolution. The dimeric N-protein structure is similar to the previously determined structure of the N protein from PRRSV, with most differences localized to the terminal helices and flexible loops. The N protein is organized as dimers of dimers in the crystal, which may reflect the arrangement of the protein in the viral nucleocapsid.

PubMed: 17452783
DOI: 10.1107/S0907444907008372

Experimental method

X-RAY DIFFRACTION (2 Å)