1P65
Crystal structure of the nucleocapsid protein of porcine reproductive and respiratory syndrome virus (PRRSV)
Summary for 1P65
| Entry DOI | 10.2210/pdb1p65/pdb |
| Descriptor | nucleocapsid protein (2 entities in total) |
| Functional Keywords | virus, nucleocapsid, viral protein |
| Biological source | Porcine respiratory and reproductive syndrome virus |
| Total number of polymer chains | 2 |
| Total formula weight | 16344.06 |
| Authors | Doan, D.N.P.,Dokland, T. (deposition date: 2003-04-29, release date: 2003-11-25, Last modification date: 2024-02-14) |
| Primary citation | Doan, D.N.P.,Dokland, T. Structure of the nucleocapsid protein of porcine reproductive and respiratory syndrome virus. Structure, 11:1445-1451, 2003 Cited by PubMed Abstract: Porcine reproductive and respiratory syndrome virus (PRRSV) is an enveloped RNA virus of the Arteriviridae family, genomically related to the coronaviruses. PRRSV is the causative agent of both severe and persistent respiratory disease and reproductive failure in pigs worldwide. The PRRSV virion contains a core made of the 123 amino acid nucleocapsid (N) protein, a product of the ORF7 gene. We have determined the crystal structure of the capsid-forming domain of N. The structure was solved to 2.6 A resolution by SAD methods using the anomalous signal from sulfur. The N protein exists in the crystal as a tight dimer forming a four-stranded beta sheet floor superposed by two long alpha helices and flanked by two N- and two C-terminal alpha helices. The structure of N represents a new class of viral capsid-forming domains, distinctly different from those of other known enveloped viruses, but reminiscent of the coat protein of bacteriophage MS2. PubMed: 14604534DOI: 10.1016/j.str.2003.09.018 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
Download full validation report
