5i62 | pdb_00005i62

Crystal structure of the insertion loop deletion mutant of the RNA-dependent RNA polymerase of a human picorbirnavirus

spinqualitylabelsall models 5i62, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5i62 is a 1 chain structure with sequence from Human picobirnavirus strain Hy005102. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.001Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RDRP_HPBVH RNA-directed RNA polymerase that is involved in both transcription and genome replication. Publication Abstract from PubMed During the replication cycle of double-stranded (ds) RNA viruses, the viral RNA-dependent RNA polymerase (RdRP) replicates and transcribes the viral genome from within the viral capsid. How the RdRP molecules are packaged within the virion and how they function within the confines of an intact capsid are intriguing questions with answers that most likely vary across the different dsRNA virus families. In this study, we have determined a 2.4 A resolution structure of an RdRP from the human picobirnavirus (hPBV). In addition to the conserved polymerase fold, the hPBV RdRP possesses a highly flexible 24 amino acid loop structure located near the C-terminus of the protein that is inserted into its active site. In vitro RNA polymerization assays and site-directed mutagenesis showed that: (1) the hPBV RdRP is fully active using both ssRNA and dsRNA templates; (2) the insertion loop likely functions as an assembly platform for the priming nucleotide to allow de novo initiation; (3) RNA transcription by the hPBV RdRP proceeds in a semi-conservative manner; and (4) the preference of virus-specific RNA during transcription is dictated by the lower melting temperature associated with the terminal sequences. Co-expression of the hPBV RdRP and the capsid protein (CP) indicated that, under the conditions used, the RdRP could not be incorporated into the recombinant capsids in the absence of the viral genome. Additionally, the hPBV RdRP exhibited higher affinity towards the conserved 5'-terminal sequence of the viral RNA, suggesting that the RdRP molecules may be encapsidated through their specific binding to the viral RNAs during assembly. Initiation of RNA Polymerization and Polymerase Encapsidation by a Small dsRNA Virus.,Collier AM, Lyytinen OL, Guo YR, Toh Y, Poranen MM, Tao YJ PLoS Pathog. 2016 Apr 14;12(4):e1005523. doi: 10.1371/journal.ppat.1005523., eCollection 2016 Apr. PMID:27078841 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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