Extended Data Fig. 9: Conformational changes associated with the ligand binding to apo PsCap5 dimer.
From: Activation of CBASS Cap5 endonuclease immune effector by cyclic nucleotides
a, Overlay of apo PsCap5 A/B dimer and dimer A/B in the ligand-bound activated PsCap5 tetramer. The structure of apo PsCap5 crisscross dimer with the SAVED domains in the “open” conformation is colored light gray. The structure of the ligand-bound dimer (protomers A and B; one of the two dimers in the tetramer) is colored in cyan for protomer A and beige for protomer B and shown in the same view as in Fig. 5. The structures are superimposed by the HNH endonuclease domains of protomers A and B. The SAVED of protomer A rotates by 160° and presents the opposite surface to the SAVED of protomer B with the β9-α10 structural element facing inward. Protomer B on the other hand rotates by 82° with the β9-α10 structural element facing outward. b and c, Vector map of global conformational changes upon the activating ligand binding to apo PsCap5 for protomers A and B, respectively.
