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. 2020 Jul 17;11:3590. doi: 10.1038/s41467-020-17349-4

Fig. 3. LACV-L CBD structure and its interaction with the endonuclease.

Fig. 3

a LACV-L CBD atomic model. Secondary structures are shown. The fold conserved with other sNSV CBD is shown in red and yellow. LACV CBD insertion is shown in orange. The missing loop comprising the active site is shown as a dotted line. b Multiple alignment of six Peribunyaviridae CBD: La Crosse virus (LACV), Bunyamwera virus (BUNYW), Schmallenberg (SVBVH), Macaua virus (MCAV), Wolkberg virus (WBV), and Oya virus. Secondary structures of LACV-L CBD are shown and colored as in a. Missing residues of LACV-L CBD are presented as dotted lines. Conserved residues of Peribunyaviridae CBD active site motif (WNxWQxxR) are shown as orange stars. c Cryo-EM 3D classes corresponding to LACV-L CBD extreme position 1 and 2 are superimposed. CBD movement is compared to LACV-L core and endonuclease that adopt stable positions. Their CBD are, respectively, shown in blue and purple. The endonuclease domain is shown in green. LACV-L core is shown in gray. d Overview and close-up view of the CBD/endonuclease domain interactions in the extreme position 1. Interacting residues are identified and labeled. CBD coloring is the same as in a. e Overview of the CBD/endonuclease domain interaction in the extreme position 2. Interacting residues are identified and labeled. CBD side chain positions remain however hypothetical due to the CBD EM map resolution in extreme position 2.