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 the segmented genome and RNA polymerase complex inside a dsRNA virus.
Journal, issue, pages	Nature, Vol. 527, Issue 7579, Page 531-534, Year 2015
Publish date	Nov 26, 2015
Authors	Xing Zhang / Ke Ding / Xuekui Yu / Winston Chang / Jingchen Sun / Z Hong Zhou /
PubMed Abstract	Viruses in the Reoviridae, like the triple-shelled human rotavirus and the single-shelled insect cytoplasmic polyhedrosis virus (CPV), all package a genome of segmented double-stranded RNAs (dsRNAs) ...Viruses in the Reoviridae, like the triple-shelled human rotavirus and the single-shelled insect cytoplasmic polyhedrosis virus (CPV), all package a genome of segmented double-stranded RNAs (dsRNAs) inside the viral capsid and carry out endogenous messenger RNA synthesis through a transcriptional enzyme complex (TEC). By direct electron-counting cryoelectron microscopy and asymmetric reconstruction, we have determined the organization of the dsRNA genome inside quiescent CPV (q-CPV) and the in situ atomic structures of TEC within CPV in both quiescent and transcribing (t-CPV) states. We show that the ten segmented dsRNAs in CPV are organized with ten TECs in a specific, non-symmetric manner, with each dsRNA segment attached directly to a TEC. The TEC consists of two extensively interacting subunits: an RNA-dependent RNA polymerase (RdRP) and an NTPase VP4. We find that the bracelet domain of RdRP undergoes marked conformational change when q-CPV is converted to t-CPV, leading to formation of the RNA template entry channel and access to the polymerase active site. An amino-terminal helix from each of two subunits of the capsid shell protein (CSP) interacts with VP4 and RdRP. These findings establish the link between sensing of environmental cues by the external proteins and activation of endogenous RNA transcription by the TEC inside the virus.
External links	Nature / PubMed:26503045 / PubMed Central
Methods	EM (single particle)
Resolution	3.3 - 22.0 Å
Structure data	6404 3jb7 EMDB-6404, PDB-3jb7: In situ structures of the segmented genome and RNA polymerase complex inside a dsRNA virus Method: EM (single particle) / Resolution: 4.0 Å EMDB-6405: In situ structures of the segmented genome and RNA polymerase complex inside a dsRNA virus Method: EM (single particle) / Resolution: 4.0 Å EMDB-6406: In situ structures of the segmented genome and RNA polymerase complex inside a dsRNA virus Method: EM (single particle) / Resolution: 3.3 Å EMDB-6407: In situ structures of the segmented genome and RNA polymerase complex inside a dsRNA virus Method: EM (single particle) / Resolution: 3.3 Å 6408 3jb6 EMDB-6408, PDB-3jb6: In situ structures of the segmented genome and RNA polymerase complex inside a dsRNA virus Method: EM (single particle) / Resolution: 3.3 Å EMDB-6409: In situ structures of the segmented genome and RNA polymerase complex inside a dsRNA virus Method: EM (single particle) / Resolution: 22.0 Å
Chemicals	ChemComp-GTP: GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying moleculeYM ChemComp-CTP*: CYTIDINE-5'-TRIPHOSPHATE
Source	bombyx mori cypovirus 1 Bombyx mori (domestic silkworm)
Keywords	TRANSFERASE/VIRAL PROTEIN / dsRNA genome organization / viral polymerase / TRANSFERASE-VIRAL PROTEIN complex / TRANSFERASE/VIRAL PROTEIN/RNA / TRANSFERASE-VIRAL PROTEIN-RNA complex