PDBsum entry 6s2c

Virus

PDB id: 6s2c

Contents

Protein chains

830 a.a.

PDB id:

6s2c

Name:

Virus

Title:

Acquired functional capsid structures in metazoan totivirus-like dsrna virus.

Structure:

Capsid protein. Chain: a. Capsid protein. Chain: b

Source:

Omono river virus. Organism_taxid: 753758. Organism_taxid: 753758

Authors:

K.Okamoto,S.D.D.Larsson,R.N.C.F.Maia,K.Murata,J.Hajdu,K.Iwasaki, N.Miyazaki

Key ref:

K.Okamoto et al. (2020). Acquired Functional Capsid Structures in Metazoan Totivirus-like dsRNA Virus. Structure, 28, 888. PubMed id: 32413288 DOI: 10.1016/j.str.2020.04.016

Date:

20-Jun-19 Release date: 29-Apr-20

Protein chains

E1CI69  (E1CI69_9VIRU) -  Capsid protein from Omono River virus

Seq: 1685 a.a.

Struc: 830 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.str.2020.04.016

Structure 28:888 (2020)

PubMed id: 32413288

Acquired Functional Capsid Structures in Metazoan Totivirus-like dsRNA Virus.

K.Okamoto, R.J.Ferreira, D.S.D.Larsson, F.R.N.C.Maia, H.Isawa, K.Sawabe, K.Murata, J.Hajdu, K.Iwasaki, P.M.Kasson, N.Miyazaki.

ABSTRACT

Non-enveloped icosahedral double-stranded RNA (dsRNA) viruses possess multifunctional capsids required for their proliferation. Whereas protozoan/fungal dsRNA viruses have a relatively simple capsid structure, which suffices for the intracellular phase in their life cycle, metazoan dsRNA viruses have acquired additional structural features as an adaptation for extracellular cell-to-cell transmission in multicellular hosts. Here, we present the first atomic model of a metazoan dsRNA totivirus-like virus and the structure reveals three unique structural traits: a C-terminal interlocking arm, surface projecting loops, and an obstruction at the pore on the 5-fold symmetry axis. These traits are keys to understanding the capsid functions of metazoan dsRNA viruses, such as particle stability and formation, cell entry, and endogenous intraparticle transcription of mRNA. On the basis of molecular dynamics simulations of the obstructed pore, we propose a possible mechanism of intraparticle transcription in totivirus-like viruses, which dynamically switches between open and closed states of the pore(s).