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5YKV

The crystal structure of Macrobrachium rosenbergii nodavirus P-domain

5YKV の概要
エントリーDOI10.2210/pdb5ykv/pdb
分子名称Capsid protein (2 entities in total)
機能のキーワードviral capsid protein, viral protein
由来する生物種Macrobrachium rosenbergii nodavirus (MrNV)
タンパク質・核酸の鎖数8
化学式量合計110667.87
構造登録者
Chen, N.C.,Yoshimura, M.,Lin, C.C.,Guan, H.H.,Chuankhayan, P.,Chen, C.J. (登録日: 2017-10-16, 公開日: 2018-10-24, 最終更新日: 2024-03-27)
主引用文献Chen, N.C.,Yoshimura, M.,Miyazaki, N.,Guan, H.H.,Chuankhayan, P.,Lin, C.C.,Chen, S.K.,Lin, P.J.,Huang, Y.C.,Iwasaki, K.,Nakagawa, A.,Chan, S.I.,Chen, C.J.
The atomic structures of shrimp nodaviruses reveal new dimeric spike structures and particle polymorphism.
Commun Biol, 2:72-72, 2019
Cited by
PubMed Abstract: Shrimp nodaviruses, including (PvNV) and nodaviruses (MrNV), cause white-tail disease in shrimps, with high mortality. The viral capsid structure determines viral assembly and host specificity during infections. Here, we show cryo-EM structures of  = 3 and  = 1 PvNV-like particles (PvNV-LPs), crystal structures of the protrusion-domains (P-domains) of PvNV and MrNV, and the crystal structure of the ∆N-ARM-PvNV shell-domain (S-domain) in  = 1 subviral particles. The capsid protein of PvNV reveals five domains: the P-domain with a new jelly-roll structure forming cuboid-like spikes; the jelly-roll S-domain with two calcium ions; the linker between the S- and P-domains exhibiting new cross and parallel conformations; the N-arm interacting with nucleotides organized along icosahedral two-fold axes; and a disordered region comprising the basic -terminal arginine-rich motif (N-ARM) interacting with RNA. The N-ARM controls  = 3 and  = 1 assemblies. Increasing the /-termini flexibility leads to particle polymorphism. Linker flexibility may influence the dimeric-spike arrangement.
PubMed: 30820467
DOI: 10.1038/s42003-019-0311-z
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.31 Å)
構造検証レポート
Validation report summary of 5ykv
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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