2FQM

Crystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus

2FQM の概要

• エントリーDOI: 10.2210/pdb2fqm/pdb
• 分子名称: Phosphoprotein (2 entities in total)
• 機能のキーワード: negative strand rna virus, polymerase, replication, cofactor, viral protein
• 由来する生物種: Vesicular stomatitis Indiana virus
• 細胞内の位置: Virion: P04880
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 50655.41

構造登録者

Ding, H.,Green, T.J.,Lu, S.,Luo, M. (登録日: 2006-01-18, 公開日: 2006-02-07, 最終更新日: 2024-02-14)

主引用文献

Ding, H.,Green, T.J.,Lu, S.,Luo, M.
Crystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus
J.Virol., 80:2808-2814, 2006

PubMed Abstract: In the replication cycle of nonsegmented negative-strand RNA viruses, the viral RNA-dependent RNA polymerase (L) recognizes a nucleoprotein (N)-enwrapped RNA template during the RNA polymerase reaction. The viral phosphoprotein (P) is a polymerase cofactor essential for this recognition. We report here the 2.3-angstroms-resolution crystal structure of the central domain (residues 107 to 177) of P from vesicular stomatitis virus. The fold of this domain consists of a beta hairpin, an alpha helix, and another beta hairpin. The alpha helix provides the stabilizing force for forming a homodimer, while the two beta hairpins add additional stabilization by forming a four-stranded beta sheet through domain swapping between two molecules. This central dimer positions the N- and C-terminal domains of P to interact with the N and L proteins, allowing the L protein to specifically recognize the nucleocapsid-RNA template and to progress along the template while concomitantly assembling N with nascent RNA. The interdimer interactions observed in the noncrystallographic packing may offer insight into the mechanism of the RNA polymerase processive reaction along the viral nucleocapsid-RNA template.

PubMed: 16501089
DOI: 10.1128/JVI.80.6.2808-2814.2006

実験手法

X-RAY DIFFRACTION (2.3 Å)