Fig. 1: Cryo-EM structure of the RSV polymerase in complex with the leader (Le10) promoter of the RSV genome. | Nature

Fig. 1: Cryo-EM structure of the RSV polymerase in complex with the leader (Le10) promoter of the RSV genome.

From: Structures of the promoter-bound respiratory syncytial virus polymerase

Fig. 1

a, Schematic representation of the RSV polymerase (L–P complex) with labelled domain boundaries and P regions interacting with N0 (RNA-free N), M2-1, N (RNA-bound N) and L proteins. The domains with missing density are coloured grey. The key residues for each functional domain are highlighted above with blue and underlined residue numbers. AU, absorbance units. b, The size-exclusion chromatography and SDS–polyacrylamide gel electrophoresis (PAGE) gel results show the quality and purity of the purified RSV L–P complex. All data shown are representative of three independent experiments (n = 3), and the uncropped SDS–PAGE image is shown in Supplementary Fig. 1. c, The sequence and structure of the Le10 RNA template in the Le10-bound RSV polymerase. The residues are labelled as the template (T) position number and base name. d, Schematic diagrams of the RSV polymerase in complex with Le10 in two orientations. The atomic model of the RdRp domain (blue) and the Cap domain (green) of RSV L, as well as POD (red) and PCTD (orange) of a tetramer of RSV P, are shown. The POD and PCTD domains of each P monomer are labelled as P1, P2, P3 and P4. The missing domains (coloured grey) include the CD, the MT domain and the CTD of RSV L, and the PNTD of RSV P. The domains are colour-coded, as in a, and the Le10 RNA template is coloured yellow, as in c. The ‘GDN’ motif (residues 810–812) from the RdRp domain is shown as magenta spheres, and the ‘HR’ motif (residues 1338–1339) from the Cap domain is shown as light brown spheres.

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