Fig. 5: The conformational change of the SAVI-related mutant V147L.

a The density map of the mutant V147L. The two monomers are colored in green and blue, respectively. b A ribbon representation of the mutant V147L. The two monomers are colored as in a. c Structural alignments of the apo STING (PDB 6NT5, grey), the HB3089-bound STING (this study, red), and STING mutant V147L (this study, blue and green). The proteins are displayed in ribbon. The HB3089 is in stick. d A top of the red boxed region in c, showing the LBD of the mutant is slightly less contracted than that of the HB3089-bound form. e The inter-Cα distance between residues His185 at LBDα1 of the mutant V147L. f Side (left) and top (right) view of the connector from HB3089-bound STING, showing the two monomers of the connector and the LBDα1 form the right-handed crossover. The map and model are in transparent surface and ribbon, respectively. Side view (g) and top (h) view of the orange boxed region in c, showing the helices and the loops of the connector from the mutant (green and blue) revolved (curved arrows) and moved downwards (arrows), respectively. The residues 147 are indicated by side chain showing. i The inter-Cα distance between residues Leu147 at the connector of the mutant V147L. j A top view of the boxed region in c. The conformational changes of the TMD of the mutant is essentially identical to that of the HB3089-bound form as describe in Fig. 2b. The side (k) and top (l) views of the boxed view in c, showing that the TM1 revolved on its own axis as compared that of the apo STING. It shows that the TM1 of the mutant V147L revolved on its own axis, which is similar to that of agonist-bound STING. For clarify, only the TM1 and TM4 are shown.