7yed

In situ structure of polymerase complex of mammalian reovirus in the elongation state

spinqualitylabelsall models 7yed, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7yed is a 25 chain structure with sequence from Mammalian orthoreovirus 3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3Å Ligands: GTP, MG, SAM, UTP, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C9E874_9REOV Publication Abstract from PubMed Mammalian reovirus (reovirus) is a multilayered, turreted member of Reoviridae characterized by transcription of dsRNA genome within the innermost capsid shell. Here, we present high-resolution in situ structures of reovirus transcriptase complex in an intact double-layered virion, and in the uncoated single-layered core particles in the unloaded, reloaded, pre-elongation, and elongation states, respectively, obtained by cryo-electron microscopy and sub-particle reconstructions. At the template entry of RNA-dependent RNA polymerase (RdRp), the RNA-loading region gets flexible after uncoating resulting in the unloading of terminal genomic RNA and inactivity of transcription. However, upon adding transcriptional substrates, the RNA-loading region is recovered leading the RNAs loaded again. The priming loop in RdRp was found to play a critical role in regulating transcription, which hinders the elongation of transcript in virion and triggers the rearrangement of RdRp C-terminal domain (CTD) during elongation, resulting in splitting of template-transcript hybrid and opening of transcript exit. With the integration of these structures, a transcriptional model of reovirus with five states is proposed. Our structures illuminate the RdRp activation and regulation of the multilayered turreted reovirus. In situ structures of polymerase complex of mammalian reovirus illuminate RdRp activation and transcription regulation.,Bao K, Zhang X, Li D, Sun W, Sun Z, Wang J, Zhu P Proc Natl Acad Sci U S A. 2022 Dec 13;119(50):e2203054119. doi: , 10.1073/pnas.2203054119. Epub 2022 Dec 5. PMID:36469786 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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