4BGP

Crystal structure of La Crosse virus nucleoprotein

4BGP の概要

• エントリーDOI: 10.2210/pdb4bgp/pdb
• 関連するPDBエントリー: 4BHH
• 分子名称: NUCLEOPROTEIN, GLYCEROL, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: viral protein, orthobunyavirus, nucleoprotein
• 由来する生物種: LA CROSSE VIRUS
• 細胞内の位置: Virion: P04873
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26980.61

構造登録者

Reguera, J.,Malet, H.,Weber, F.,Cusack, S. (登録日: 2013-03-28, 公開日: 2013-04-24, 最終更新日: 2024-11-13)

主引用文献

Reguera, J.,Malet, H.,Weber, F.,Cusack, S.
Structural Basis for Encapsidation of Genomic RNA by La Crosse Orthobunyavirus Nucleoprotein
Proc.Natl.Acad.Sci.USA, 110:7246-, 2013

PubMed Abstract: The nucleoprotein (NP) of segmented negative-strand RNA viruses such as Orthomyxo-, Arena-, and Bunyaviruses coats the genomic viral RNA and together with the polymerase forms ribonucleoprotein particles (RNPs), which are both the template for replication and transcription and are packaged into new virions. Here we describe the crystal structure of La Crosse Orthobunyavirus NP both RNA free and a tetrameric form with single-stranded RNA bound. La Crosse Orthobunyavirus NP is a largely helical protein with a fold distinct from other bunyavirus genera NPs. It binds 11 RNA nucleotides in the positively charged groove between its two lobes, and hinged N- and C-terminal arms mediate oligomerization, allowing variable protein-protein interface geometry. Oligomerization and RNA binding are mediated by residues conserved in the Orthobunyavirus genus. In the twofold symmetric tetramer, 44 nucleotides bind in a closed ring with sharp bends at the NP-NP interfaces. The RNA is largely inaccessible within a continuous internal groove. Electron microscopy of RNPs released from virions shows them capable of forming a hierarchy of more or less compact irregular helical structures. We discuss how the planar, tetrameric NP-RNA structure might relate to a polar filament that upon supercoiling could be packaged into virions. This work gives insight into the RNA encapsidation and protection function of bunyavirus NP, but also highlights the need for dynamic rearrangements of the RNP to give the polymerase access to the template RNA.

PubMed: 23589854
DOI: 10.1073/PNAS.1302298110

実験手法

X-RAY DIFFRACTION (1.8 Å)