6AB5
Cryo-EM structure of T=1 Penaeus vannamei nodavirus
Summary for 6AB5
Entry DOI | 10.2210/pdb6ab5/pdb |
EMDB information | 6999 9576 |
Descriptor | Capsid protein (1 entity in total) |
Functional Keywords | nodaviridae, shrimp nodavirus, virus like particle |
Biological source | Penaeus vannamei nodavirus |
Total number of polymer chains | 1 |
Total formula weight | 40262.17 |
Authors | Chen, N.C.,Miyazaki, N.,Yoshimura, M.,Guan, H.H.,Lin, C.C.,Iwasaki, K.,Chen, C.J. (deposition date: 2018-07-20, release date: 2019-03-20, Last modification date: 2024-03-27) |
Primary citation | 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 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.7 Å) |
Structure validation
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