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6AB5

Cryo-EM structure of T=1 Penaeus vannamei nodavirus

Summary for 6AB5
Entry DOI10.2210/pdb6ab5/pdb
EMDB information6999 9576
DescriptorCapsid protein (1 entity in total)
Functional Keywordsnodaviridae, shrimp nodavirus, virus like particle
Biological sourcePenaeus vannamei nodavirus
Total number of polymer chains1
Total formula weight40262.17
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 citationChen, 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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.7 Å)
Structure validation

226707

數據於2024-10-30公開中

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