2MXD

Solution structure of VPg of porcine sapovirus

2MXD の概要

• エントリーDOI: 10.2210/pdb2mxd/pdb
• NMR情報: BMRB: 25404
• 分子名称: Viral protein genome-linked (1 entity in total)
• 機能のキーワード: viral protein genome-linked, porcine sapovirus, viral protein
• 由来する生物種: Porcine enteric sapovirus
• 細胞内の位置: Capsid protein: Virion: Q9QEJ5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7382.23

構造登録者

Kim, J.,Hwang, H.,Min, H.,Yun, H.,Cho, K.,Pelton, J.G.,Wemmer, D.E.,Lee, C. (登録日: 2014-12-24, 公開日: 2015-04-15, 最終更新日: 2024-05-15)

主引用文献

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

実験手法

SOLUTION NMR