Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	In situ structures of polymerase complex of mammalian reovirus illuminate RdRp activation and transcription regulation.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 119, Issue 50, Page e2203054119, Year 2022
Publish date	Dec 13, 2022
Authors	Keyan Bao / Xueli Zhang / Dongyu Li / Wei Sun / Zhenzhao Sun / Jingfei Wang / Ping Zhu /
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 ...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.
External links	Proc Natl Acad Sci U S A / PubMed:36469786 / PubMed Central
Methods	EM (single particle)
Resolution	3.0 - 3.6 Å
Structure data	33770 7yed EMDB-33770, PDB-7yed: In situ structure of polymerase complex of mammalian reovirus in the elongation state Method: EM (single particle) / Resolution: 3.0 Å 33778 7yev EMDB-33778, PDB-7yev: In situ structure of polymerase complex of mammalian reovirus in the pre-elongation state Method: EM (single particle) / Resolution: 3.6 Å 33779 7yez EMDB-33779, PDB-7yez: In situ structure of polymerase complex of mammalian reovirus in the reloaded state Method: EM (single particle) / Resolution: 3.4 Å 33780 7yf0 EMDB-33780, PDB-7yf0: In situ structure of polymerase complex of mammalian reovirus in the core Method: EM (single particle) / Resolution: 3.4 Å 33787 7yfe EMDB-33787, PDB-7yfe: In situ structure of polymerase complex of mammalian reovirus in virion Method: EM (single particle) / Resolution: 3.4 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-SAM: S-ADENOSYLMETHIONINE ChemComp-GTP: GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying moleculeYM ChemComp-UTP: URIDINE 5'-TRIPHOSPHATE / UTPYM ChemComp-MG: Unknown entry
Source	mammalian orthoreovirus 3
Keywords	VIRAL PROTEIN/RNA / mammalian reovirus / cryo-em / RNA dependent RNA polymerase / transcription / VIRAL PROTEIN / VIRAL PROTEIN-RNA complex