2K47

Solution structure of the C-terminal N-RNA binding domain of the Vesicular Stomatitis Virus Phosphoprotein

2K47 の概要

• エントリーDOI: 10.2210/pdb2k47/pdb
• 分子名称: Phosphoprotein (1 entity in total)
• 機能のキーワード: flexible tail, chaperone, cytoplasm, phosphoprotein, rna replication, virion, replication
• 由来する生物種: Vesicular stomatitis Indiana virus (VSIV)
• 細胞内の位置: Virion: P03520
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9093.42

構造登録者

Ribeiro, E.A.,Favier, A.,Gerard, F.C.,Leyrat, C.,Brutscher, B.,Blondel, D.,Ruigrok, R.W.,Blackledge, M.,Jamin, M. (登録日: 2008-05-28, 公開日: 2008-09-09, 最終更新日: 2024-05-29)

主引用文献

Ribeiro, E.A.,Favier, A.,Gerard, F.C.,Leyrat, C.,Brutscher, B.,Blondel, D.,Ruigrok, R.W.,Blackledge, M.,Jamin, M.
Solution Structure of the C-Terminal Nucleoprotein-RNA Binding Domain of the Vesicular Stomatitis Virus Phosphoprotein.
J.Mol.Biol., 2008

PubMed Abstract: Beyond common features in their genome organization and replication mechanisms, the evolutionary relationships among viruses of the Rhabdoviridae family are difficult to decipher because of the great variability in the amino acid sequence of their proteins. The phosphoprotein (P) of vesicular stomatitis virus (VSV) is an essential component of the RNA transcription and replication machinery; in particular, it contains binding sites for the RNA-dependent RNA polymerase and for the nucleoprotein. Here, we devised a new method for defining boundaries of structured domains from multiple disorder prediction algorithms, and we identified an autonomous folding C-terminal domain in VSV P (P(CTD)). We show that, like the C-terminal domain of rabies virus (RV) P, VSV P(CTD) binds to the viral nucleocapsid (nucleoprotein-RNA complex). We solved the three-dimensional structure of VSV P(CTD) by NMR spectroscopy and found that the topology of its polypeptide chain resembles that of RV P(CTD). The common part of both proteins could be superimposed with a backbone RMSD from mean atomic coordinates of 2.6 A. VSV P(CTD) has a shorter N-terminal helix (alpha(1)) than RV P(CTD); it lacks two alpha-helices (helices alpha(3) and alpha(6) of RV P), and the loop between strands beta(1) and beta(2) is longer than that in RV. Dynamical properties measured by NMR relaxation revealed the presence of fast motions (below the nanosecond timescale) in loop regions (amino acids 209-214) and slower conformational exchange in the N- and C-terminal helices. Characterization of a longer construct indicated that P(CTD) is preceded by a flexible linker. The results presented here support a modular organization of VSV P, with independent folded domains separated by flexible linkers, which is conserved among different genera of Rhabdoviridae and is similar to that proposed for the P proteins of the Paramyxoviridae.

PubMed: 18657547
DOI: 10.1016/j.jmb.2008.07.028

実験手法

SOLUTION NMR