@article {65277,
	title = {Structure of the vesicular stomatitis virus L protein in complex with Its phosphoprotein cofactor.},
	journal = {Cell Reports},
	volume = {30},
	year = {2020},
	month = {2020 Jan 07},
	pages = {53-60.e5},
	abstract = {<p>The large (L) proteins of non-segmented, negative-strand RNA viruses are multifunctional enzymes that produce capped, methylated, and polyadenylated mRNA and replicate the viral genome. A phosphoprotein (P), required for efficient RNA-dependent RNA polymerization from the viral ribonucleoprotein (RNP) template, regulates the function and conformation of the L protein. We report the structure of vesicular stomatitis virus L in complex with its P cofactor determined by electron cryomicroscopy at 3.0\&nbsp;{\r A} resolution, enabling us to visualize bound segments of P. The contacts of three P segments with multiple L domains show how P induces a closed, compact, initiation-competent conformation. Binding of P to L positions its N-terminal domain adjacent to a putative RNA exit channel for efficient encapsidation of newly synthesized genomes with the nucleoprotein and orients its C-terminal domain to interact with an RNP template. The model shows that a conserved tryptophan in the priming loop can support the initiating 5{\textquoteright} nucleotide.</p>
},
	issn = {2211-1247},
	doi = {10.1016/j.celrep.2019.12.024},
	author = {Jenni, Simon and Bloyet, Louis-Marie and Diaz-Avalos, Ruben and Liang, Bo and Whelan, Sean P J and Grigorieff, Nikolaus and Harrison, Stephen C}
}
