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. Author manuscript; available in PMC: 2020 May 7.
Published in final edited form as: Nature. 2019 Nov 7;577(7789):275–279. doi: 10.1038/s41586-019-1759-1

Figure 2. Structure of the HMPV L protein.

Figure 2.

(a) The RdRp viewed in its “front” orientation. Fingers subdomain: blue; palm: red and thumb: green, NTD: grey. RdRp motifs A-G are shown. (b) The capping domain of L (green ribbons) of HMPV-L. A superposition of HMPV-L with VSV-L3 (grey ribbons) highlights the difference between conformations of the putative priming loops: putative priming loop of HMPV-L (including Thr1192 of the GxxT motif): red and of VSV-L (1157–1173): gold. P: magenta. (c) RNA capping motifs A’-E’.2 (d) Overall view of HMPV-L with VSV-L superimposed, highlighting the mobile appendage (displayed in the VSV-L orientation, but disordered in the present structure) and rNTP (S) entry, template (T) and nascent (U) RNA tunnels. (e) Impact of substitutions in aromatic and proline residues in the putative priming loop of RSV-L on RNA production from the +1 and +3 sites. The mean and standard error of three independent experiments are indicated. (f) Sequence conservation in the putative priming loop of L. The four residues that were mutated (panel e) are indicated by arrows. A proline residue (P1186 in HMPV-L) important for an early stage of RNA synthesis is conserved in Pneumoviridae, Paramyxoviridae and Filoviridae but not in Rhabdoviridae.