8iib

Crystal structure of Israeli acute paralysis virus RNA-dependent RNA polymerase delta85 mutant (residues 86-546)

spinqualitylabelsall models 8iib, resolution 2.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8iib is a 2 chain structure with sequence from Israeli acute paralysis virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.69Å Ligands: CD, CL, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 Delta85 and Delta40, both missing the NE region, and the 3D(pol) protein in these structures exhibited three conformational states. The palm and thumb domains of these IAPV 3D(pol) structures are largely consistent with those of the PV 3D(pol) structures. However, in all structures, the RdRP fingers domain is partially disordered, while different conformations of RdRP substructures and interactions between them are also present. In particular, a large-scale conformational change occurred in the motif B-middle finger region in one protein chain of the Delta40 structure, while a previously documented alternative conformation of motif A was observed in all IAPV structures. These experimental data on one hand show intrinsic conformational variances of RdRP substructures, and on the other hand suggest possible contribution of the NE region in proper RdRP folding in IAPV. Unusual substructure conformations observed in crystal structures of a dicistrovirus RNA-dependent RNA polymerase suggest contribution of the N-terminal extension in proper folding.,Fang X, Lu G, Deng Y, Yang S, Hou C, Gong P Virol Sin. 2023 May 6:S1995-820X(23)00050-0. doi: 10.1016/j.virs.2023.05.002. PMID:37156298 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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