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	Conformational changes in Lassa virus L protein associated with promoter binding and RNA synthesis activity.
Journal, issue, pages	Nat Commun, Vol. 12, Issue 1, Page 7018, Year 2021
Publish date	Dec 2, 2021
Authors	Tomas Kouba / Dominik Vogel / Sigurdur R Thorkelsson / Emmanuelle R J Quemin / Harry M Williams / Morlin Milewski / Carola Busch / Stephan Günther / Kay Grünewald / Maria Rosenthal / Stephen Cusack /
PubMed Abstract	Lassa virus is endemic in West Africa and can cause severe hemorrhagic fever. The viral L protein transcribes and replicates the RNA genome via its RNA-dependent RNA polymerase activity. Here, we ...Lassa virus is endemic in West Africa and can cause severe hemorrhagic fever. The viral L protein transcribes and replicates the RNA genome via its RNA-dependent RNA polymerase activity. Here, we present nine cryo-EM structures of the L protein in the apo-, promoter-bound pre-initiation and active RNA synthesis states. We characterize distinct binding pockets for the conserved 3' and 5' promoter RNAs and show how full-promoter binding induces a distinct pre-initiation conformation. In the apo- and early elongation states, the endonuclease is inhibited by two distinct L protein peptides, whereas in the pre-initiation state it is uninhibited. In the early elongation state, a template-product duplex is bound in the active site cavity together with an incoming non-hydrolysable nucleotide and the full C-terminal region of the L protein, including the putative cap-binding domain, is well-ordered. These data advance our mechanistic understanding of how this flexible and multifunctional molecular machine is activated.
External links	Nat Commun / PubMed:34857749 / PubMed Central
Methods	EM (single particle)
Resolution	2.7 - 3.89 Å
Structure data	12807 7och EMDB-12807, PDB-7och: Apo-structure of Lassa virus L protein (well-resolved polymerase core) [APO-CORE] Method: EM (single particle) / Resolution: 3.14 Å 12860 7oe3 EMDB-12860, PDB-7oe3: Apo-structure of Lassa virus L protein (well-resolved endonuclease) [APO-ENDO] Method: EM (single particle) / Resolution: 3.35 Å 12861 7oe7 EMDB-12861, PDB-7oe7: Apo-structure of Lassa virus L protein (well-resolved alpha ribbon) [APO-RIBBON] Method: EM (single particle) / Resolution: 3.73 Å 12862 7oea EMDB-12862, PDB-7oea: Lassa virus L protein bound to 3' promoter RNA (well-resolved polymerase core) [3END-CORE] Method: EM (single particle) / Resolution: 2.7 Å 12863 7oeb EMDB-12863, PDB-7oeb: Lassa virus L protein bound to 3' promoter RNA (well-resolved endonuclease) [3END-ENDO] Method: EM (single particle) / Resolution: 3.04 Å 12953 7ojj EMDB-12953, PDB-7ojj: Lassa virus L protein with endonuclease and C-terminal domains in close proximity [MID-LINK] Method: EM (single particle) / Resolution: 3.5 Å 12954 7ojk EMDB-12954, PDB-7ojk: Lassa virus L protein bound to the distal promoter duplex [DISTAL-PROMOTER] Method: EM (single particle) / Resolution: 3.89 Å 12955 7ojl EMDB-12955, PDB-7ojl: Lassa virus L protein in a pre-initiation conformation [PREINITIATION] Method: EM (single particle) / Resolution: 3.3 Å 12956 7ojn EMDB-12956, PDB-7ojn: Lassa virus L protein in an elongation conformation [ELONGATION] Method: EM (single particle) / Resolution: 2.92 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-MG: Unknown entry ChemComp-HOH: WATER ChemComp-MN: Unknown entry ChemComp-2KH: 5'-O-[(S)-hydroxy{[(S)-hydroxy(phosphonooxy)phosphoryl]amino}phosphoryl]uridine
Source	lassa mammarenavirus
Keywords	VIRAL PROTEIN / Lassa virus RNA-dependent RNA polymerase viral RNA