3R0R

The 2.3 A structure of porcine circovirus 2

Summary for 3R0R

• Entry DOI: 10.2210/pdb3r0r/pdb
• Descriptor: Porcine circovirus 2 (PCV2) capsid protein, SULFATE ION (3 entities in total)
• Functional Keywords: viral jelly roll, beta barrel, ssdna, virus
• Biological source: Porcine circovirus 2 (PCV2)
• Total number of polymer chains: 1
• Total formula weight: 26519.47

Authors

Khayat, R.,Speir, J.A.,Johnson, J.E. (deposition date: 2011-03-08, release date: 2011-06-15, Last modification date: 2024-02-21)

Primary citation

Khayat, R.,Brunn, N.,Speir, J.A.,Hardham, J.M.,Ankenbauer, R.G.,Schneemann, A.,Johnson, J.E.
The 2.3-angstrom structure of porcine circovirus 2.
J.Virol., 85:7856-7862, 2011

PubMed Abstract: Porcine circovirus 2 (PCV2) is a T=1 nonenveloped icosahedral virus that has had severe impact on the swine industry. Here we report the crystal structure of an N-terminally truncated PCV2 virus-like particle at 2.3-Å resolution, and the cryo-electron microscopy (cryo-EM) image reconstruction of a full-length PCV2 virus-like particle at 9.6-Å resolution. This is the first atomic structure of a circovirus. The crystal structure revealed that the capsid protein fold is a canonical viral jelly roll. The loops connecting the strands of the jelly roll define the limited features of the surface. Sulfate ions interacting with the surface and electrostatic potential calculations strongly suggest a heparan sulfate binding site that allows PCV2 to gain entry into the cell. The crystal structure also allowed previously determined epitopes of the capsid to be visualized. The cryo-EM image reconstruction showed that the location of the N terminus, absent in the crystal structure, is inside the capsid. As the N terminus was previously shown to be antigenic, it may externalize through viral "breathing."

PubMed: 21632760
DOI: 10.1128/JVI.00737-11

Experimental method

X-RAY DIFFRACTION (2.35 Å)