Unusual substructure conformations observed in crystal structures of a dicistrovirus RNA-dependent RNA polymerase suggest contribution of the N-terminal extension in proper folding.

ABSTRACT: The Dicistroviridae is a virus family that includes many insect pathogens. These viruses contain a positive-sense RNA genome that is replicated by the virally encoded RNA-dependent RNA polymerase (RdRP) also named 3D^pol. Compared with the Picornaviridae RdRPs such as poliovirus (PV) 3D^pol, the Dicistroviridae representative Israeli acute paralysis virus (IAPV) 3D^pol has an additional N-terminal extension (NE) region that is about 40-residue in length. To date, both the structure and catalytic mechanism of the Dicistroviridae RdRP have remain elusive. Here we reported crystal structures of two truncated forms of IAPV 3D^pol, namely Δ85 and Δ40, both missing the NE region, and the 3D^pol protein in these structures exhibited three conforma

SUBMITTER: Fang X 

PROVIDER: S-EPMC10436059 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature