Skip to main content
. Author manuscript; available in PMC: 2020 May 11.
Published in final edited form as: Cell Rep. 2020 Jan 7;30(1):153–163.e5. doi: 10.1016/j.celrep.2019.12.020

Figure 4. Conformational Dynamics C-Terminal α6 Helix of SFTSV L Protein Modulates Its Endonuclease Activity.

Figure 4.

(A) Dynamic simulation of SFTSV L 1–231 aa. The C-terminal α6 helix (colored in blue) is predicted to be very flexible.

(B) The average solvent accessible surface area (SASA) of each residue in SFTSV L 1–231 aa.

(C) Deuterium uptake in SFTSVL1–231 aa from HDX-MS. The deuterium uptake on SFTSV L1–231 aa is mapped onto its sequence and secondary structure with color for exchange time at 120 s of exposure in a D2O buffer (Figure S5). Groups of residues with similar differential deuterium exchange rates are colored according to a gradient for HDX-MS rates in Figure S5.

(D) FRET-based endonuclease assays of SFTSV L 1–231 aa (black) and SFTSV L 1–208 aa (red). Experiments were carried out in triplicate and average data are shown with error bars representing the standard deviation.