4IRY

Influenza A virus tail-loop free nucleoprotein at 2.8 A resolution

4IRY の概要

• エントリーDOI: 10.2210/pdb4iry/pdb
• 分子名称: Nucleocapsid protein (1 entity in total)
• 機能のキーワード: nucleoprotein, oligomerization, rna binding, rnp assembly, rna, nucleus, viral protein
• 由来する生物種: Influenza A virus; 詳細
• 細胞内の位置: Host nucleus : Q1K9H2
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 109495.42

構造登録者

Ye, Q.,Mata, D.A.,Tao, Y.J. (登録日: 2013-01-15, 公開日: 2013-02-13, 最終更新日: 2023-09-20)

主引用文献

Ye, Q.,Guu, T.S.,Mata, D.A.,Kuo, R.L.,Smith, B.,Krug, R.M.,Tao, Y.J.
Biochemical and structural evidence in support of a coherent model for the formation of the double-helical influenza a virus ribonucleoprotein.
MBio, 4:e00467-12-e00467-12, 2012

PubMed Abstract: Influenza A virions contain eight ribonucleoproteins (RNPs), each comprised of a negative-strand viral RNA, the viral polymerase, and multiple nucleoproteins (NPs) that coat the viral RNA. NP oligomerization along the viral RNA is mediated largely by a 28-amino-acid tail loop. Influenza viral RNPs, which serve as the templates for viral RNA synthesis in the nuclei of infected cells, are not linear but rather are organized in hairpin-like double-helical structures. Here we present results that strongly support a coherent model for the assembly of the double-helical influenza virus RNP structure. First, we show that NP self-associates much more weakly in the absence of RNA than in its presence, indicating that oligomerization is very limited in the cytoplasm. We also show that once NP has oligomerized, it can dissociate in the absence of bound RNA, but only at a very slow rate, indicating that the NP scaffold remains intact when viral RNA dissociates from NPs to interact with the polymerase during viral RNA synthesis. In addition, we identify a previously unknown NP-NP interface that is likely responsible for organizing the double-helical viral RNP structure. This identification stemmed from our observation that NP lacking the oligomerization tail loop forms monomers and dimers. We determined the crystal structure of this NP dimer, which reveals this new NP-NP interface. Mutation of residues that disrupt this dimer interface does not affect oligomerization of NPs containing the tail loop but does inactivate the ability of NPs containing the tail loop to support viral RNA synthesis in minigenome assays.

PubMed: 23269829
DOI: 10.1128/mBio.00467-12

実験手法

X-RAY DIFFRACTION (2.8 Å)