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-Structure paper
Title | Structure and assembly of double-headed Sendai virus nucleocapsids. |
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Journal, issue, pages | Commun Biol, Vol. 4, Issue 1, Page 494, Year 2021 |
Publish date | Apr 22, 2021 |
Authors | Na Zhang / Hong Shan / Mingdong Liu / Tianhao Li / Rui Luo / Liuyan Yang / Lei Qi / Xiaofeng Chu / Xin Su / Rui Wang / Yunhui Liu / Wenzhi Sun / Qing-Tao Shen / |
PubMed Abstract | Paramyxoviruses, including the mumps virus, measles virus, Nipah virus and Sendai virus (SeV), have non-segmented single-stranded negative-sense RNA genomes which are encapsidated by nucleoproteins ...Paramyxoviruses, including the mumps virus, measles virus, Nipah virus and Sendai virus (SeV), have non-segmented single-stranded negative-sense RNA genomes which are encapsidated by nucleoproteins into helical nucleocapsids. Here, we reported a double-headed SeV nucleocapsid assembled in a tail-to-tail manner, and resolved its helical stems and clam-shaped joint at the respective resolutions of 2.9 and 3.9 Å, via cryo-electron microscopy. Our structures offer important insights into the mechanism of the helical polymerization, in particular via an unnoticed exchange of a N-terminal hole formed by three loops of nucleoproteins, and unveil the clam-shaped joint in a hyper-closed state for nucleocapsid dimerization. Direct visualization of the loop from the disordered C-terminal tail provides structural evidence that C-terminal tail is correlated to the curvature of nucleocapsid and links nucleocapsid condensation and genome replication and transcription with different assembly forms. |
External links | Commun Biol / PubMed:33888861 / PubMed Central |
Methods | EM (single particle) / EM (helical sym.) |
Resolution | 2.9 - 4.61 Å |
Structure data | EMDB-30064: EMDB-30065: EMDB-30066: EMDB-30129: Helical stem of the cleaved double-headed nucleocapsids of sendai virus EMDB-30133: |
Source |
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Keywords | NUCLEAR PROTEIN/RNA / nucleocapsid / Sendai virus / NUCLEAR PROTEIN / NUCLEAR PROTEIN-RNA complex |