Fig. 5: Conformational flexibility of the endonuclease domain. | Nature Communications

Fig. 5: Conformational flexibility of the endonuclease domain.

From: Conformational changes in Lassa virus L protein associated with promoter binding and RNA synthesis activity

Fig. 5

a Overview of the three different conformations of the EN (orange) observed in the 3END-CORE, MID-LINK and ELONGATION structures. The EN linker (green) and the inhibitory peptide (cyan) are highlighted as well. b In the middle panel a superimposition of the EN domains of 3END-CORE (orange), corresponding also to the overall conformation of the EN domain in the MID-LINK structure, and ELONGATION (brown) with the respective positions of the inhibitory peptides in teal, cyan and light blue, respectively, is shown. Connections to the fingers domain are indicated in blue. The position of the inhibitory peptide of 3END-CORE is the same as in the APO-ENDO structure, similarly is the same position of the EN observed in both MID-LINK and DISTAL-PROMOTER structures. Right and left panels show close-ups of the autoinhibited EN active sites in the ELONGATION and 3END-CORE structures, respectively. Important residues of the protein-protein interactions are labelled and side chains are shown as sticks. For a focus on the inhibitory loop in the different conformations see Supplementary Fig. 11.

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