5YKV
The crystal structure of Macrobrachium rosenbergii nodavirus P-domain
5YKV の概要
| エントリーDOI | 10.2210/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: 30820467DOI: 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) |
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