7YED
In situ structure of polymerase complex of mammalian reovirus in the elongation state
This is a non-PDB format compatible entry.
Summary for 7YED
| Entry DOI | 10.2210/pdb7yed/pdb |
| EMDB information | 33770 |
| Descriptor | RNA helicase, GUANOSINE-5'-TRIPHOSPHATE, URIDINE 5'-TRIPHOSPHATE, ... (12 entities in total) |
| Functional Keywords | mammalian reovirus, cryo-em, rna dependent rna polymerase, transcription, viral protein, viral protein-rna complex, viral protein/rna |
| Biological source | Mammalian orthoreovirus 3 More |
| Total number of polymer chains | 25 |
| Total formula weight | 3109821.58 |
| Authors | Bao, K.Y.,Zhang, X.L.,Li, D.Y.,Zhu, P. (deposition date: 2022-07-05, release date: 2023-04-05, Last modification date: 2024-07-03) |
| Primary citation | Bao, K.,Zhang, X.,Li, D.,Sun, W.,Sun, Z.,Wang, J.,Zhu, P. In situ structures of polymerase complex of mammalian reovirus illuminate RdRp activation and transcription regulation. Proc.Natl.Acad.Sci.USA, 119:e2203054119-e2203054119, 2022 Cited by PubMed Abstract: Mammalian reovirus (reovirus) is a multilayered, turreted member of 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. PubMed: 36469786DOI: 10.1073/pnas.2203054119 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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