2MXD

Solution structure of VPg of porcine sapovirus

Summary for 2MXD

• Entry DOI: 10.2210/pdb2mxd/pdb
• NMR Information: BMRB: 25404
• Descriptor: Viral protein genome-linked (1 entity in total)
• Functional Keywords: viral protein genome-linked, porcine sapovirus, viral protein
• Biological source: Porcine enteric sapovirus
• Cellular location: Capsid protein: Virion: Q9QEJ5
• Total number of polymer chains: 1
• Total formula weight: 7382.23

Authors

Kim, J.,Hwang, H.,Min, H.,Yun, H.,Cho, K.,Pelton, J.G.,Wemmer, D.E.,Lee, C. (deposition date: 2014-12-24, release date: 2015-04-15, Last modification date: 2024-05-15)

Primary citation

Hwang, H.J.,Min, H.J.,Yun, H.,Pelton, J.G.,Wemmer, D.E.,Cho, K.O.,Kim, J.S.,Lee, C.W.
Solution structure of the porcine sapovirus VPg core reveals a stable three-helical bundle with a conserved surface patch.
Biochem.Biophys.Res.Commun., 459:610-616, 2015

PubMed Abstract: Viral protein genome-linked (VPg) proteins play a critical role in the life cycle of vertebrate and plant positive-sense RNA viruses by acting as a protein primer for genome replication and as a protein cap for translation initiation. Here we report the solution structure of the porcine sapovirus VPg core (VPg(C)) determined by multi-dimensional NMR spectroscopy. The structure of VPg(C) is composed of three α-helices stabilized by several conserved hydrophobic residues that form a helical bundle core similar to that of feline calicivirus VPg. The putative nucleotide acceptor Tyr956 within the first helix of the core is completely exposed to solvent accessible surface to facilitate nucleotidylation by viral RNA polymerase. Comparison of VPg structures suggests that the surface for nucleotidylation site is highly conserved among the Caliciviridae family, whereas the backbone core structures are different. These structural features suggest that caliciviruses share common mechanisms of VPg-dependent viral replication and translation.

PubMed: 25753201
DOI: 10.1016/j.bbrc.2015.02.156

Experimental method

SOLUTION NMR