3ZL9

Crystal structure of the nucleocapsid protein from Schmallenberg virus

3ZL9 の概要

• エントリーDOI: 10.2210/pdb3zl9/pdb
• 関連するPDBエントリー: 3ZLA
• 分子名称: NUCLEOCAPSID PROTEIN (2 entities in total)
• 機能のキーワード: viral protein, orthobunyavirus, nucleoprotein
• 由来する生物種: SCHMALLENBERG VIRUS
• 細胞内の位置: Virion: H2AM13
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 105181.48

構造登録者

Ariza, A.,Tanner, S.J.,Walter, C.T.,Dent, K.C.,Shepherd, D.A.,Wu, W.,Matthews, S.V.,Hiscox, J.A.,Green, T.J.,Luo, M.,Elliot, R.M.,Ashcroft, A.E.,Stonehouse, N.J.,Ranson, N.A.,Barr, J.N.,Edwards, T.A. (登録日: 2013-01-29, 公開日: 2013-05-01, 最終更新日: 2024-05-01)

主引用文献

Ariza, A.,Tanner, S.J.,Walter, C.T.,Dent, K.C.,Shepherd, D.A.,Wu, W.,Matthews, S.V.,Hiscox, J.A.,Green, T.J.,Luo, M.,Elliott, R.M.,Fooks, A.R.,Ashcroft, A.E.,Stonehouse, N.J.,Ranson, N.A.,Barr, J.N.,Edwards, T.A.
Nucleocapsid Protein Structures from Orthobunyaviruses Reveal Insight Into Ribonucleoprotein Architecture and RNA Polymerization.
Nucleic Acids Res., 41:5912-, 2013

PubMed Abstract: All orthobunyaviruses possess three genome segments of single-stranded negative sense RNA that are encapsidated with the virus-encoded nucleocapsid (N) protein to form a ribonucleoprotein (RNP) complex, which is uncharacterized at high resolution. We report the crystal structure of both the Bunyamwera virus (BUNV) N-RNA complex and the unbound Schmallenberg virus (SBV) N protein, at resolutions of 3.20 and 2.75 Å, respectively. Both N proteins crystallized as ring-like tetramers and exhibit a high degree of structural similarity despite classification into different orthobunyavirus serogroups. The structures represent a new RNA-binding protein fold. BUNV N possesses a positively charged groove into which RNA is deeply sequestered, with the bases facing away from the solvent. This location is highly inaccessible, implying that RNA polymerization and other critical base pairing events in the virus life cycle require RNP disassembly. Mutational analysis of N protein supports a correlation between structure and function. Comparison between these crystal structures and electron microscopy images of both soluble tetramers and authentic RNPs suggests the N protein does not bind RNA as a repeating monomer; thus, it represents a newly described architecture for bunyavirus RNP assembly, with implications for many other segmented negative-strand RNA viruses.

PubMed: 23595147
DOI: 10.1093/NAR/GKT268

実験手法

X-RAY DIFFRACTION (2.75 Å)