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	Structural insights into viral genome replication by the severe fever with thrombocytopenia syndrome virus L protein.
Journal, issue, pages	Nucleic Acids Res, Vol. 51, Issue 3, Page 1424-1442, Year 2023
Publish date	Jan 18, 2023
Authors	Harry M Williams / Sigurdur R Thorkelsson / Dominik Vogel / Morlin Milewski / Carola Busch / Stephen Cusack / Kay Grünewald / Emmanuelle R J Quemin / Maria Rosenthal /
PubMed Abstract	Severe fever with thrombocytopenia syndrome virus (SFTSV) is a phenuivirus that has rapidly become endemic in several East Asian countries. The large (L) protein of SFTSV, which includes the RNA- ...Severe fever with thrombocytopenia syndrome virus (SFTSV) is a phenuivirus that has rapidly become endemic in several East Asian countries. The large (L) protein of SFTSV, which includes the RNA-dependent RNA polymerase (RdRp), is responsible for catalysing viral genome replication and transcription. Here, we present 5 cryo-electron microscopy (cryo-EM) structures of the L protein in several states of the genome replication process, from pre-initiation to late-stage elongation, at a resolution of up to 2.6 Å. We identify how the L protein binds the 5' viral RNA in a hook-like conformation and show how the distal 5' and 3' RNA ends form a duplex positioning the 3' RNA terminus in the RdRp active site ready for initiation. We also observe the L protein stalled in the early and late stages of elongation with the RdRp core accommodating a 10-bp product-template duplex. This duplex ultimately splits with the template binding to a designated 3' secondary binding site. The structural data and observations are complemented by in vitro biochemical and cell-based mini-replicon assays. Altogether, our data provide novel key insights into the mechanism of viral genome replication by the SFTSV L protein and will aid drug development against segmented negative-strand RNA viruses.
External links	Nucleic Acids Res / PubMed:36651274 / PubMed Central
Methods	EM (single particle)
Resolution	2.6 - 3.6 Å
Structure data	15607 8as6 EMDB-15607, PDB-8as6: Structure of the SFTSV L protein bound to 5' cRNA hook [5' HOOK] Method: EM (single particle) / Resolution: 3.4 Å 15608 8as7 EMDB-15608, PDB-8as7: Structure of the SFTSV L protein stalled at early elongation [EARLY-ELONGATION] Method: EM (single particle) / Resolution: 2.6 Å 15610 8asb EMDB-15610, PDB-8asb: Structure of the SFTSV L protein stalled at early elongation with the endonuclease domain in a raised conformation [EARLY-ELONGATION-ENDO] Method: EM (single particle) / Resolution: 3.6 Å 15614 8asd EMDB-15614, PDB-8asd: Structure of the SFTSV L protein stalled at late elongation [LATE-ELONGATION] Method: EM (single particle) / Resolution: 2.6 Å 15615 8asg EMDB-15615, PDB-8asg: Structure of the SFTSV L protein bound in a resting state [RESTING] Method: EM (single particle) / Resolution: 3.2 Å
Chemicals	ChemComp-MG: Unknown entry ChemComp-EPE: 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / pH bufferYM ChemComp-2KH: 5'-O-[(S)-hydroxy{[(S)-hydroxy(phosphonooxy)phosphoryl]amino}phosphoryl]uridine ChemComp-HOH*: WATER
Source	sfts virus ah12
Keywords	VIRAL PROTEIN / SFTSV RNA-DEPENDENT RNA POLYMERASE / VIRAL RNA