Fig. 6: PPT movement mediated by rotational movements in helices H1 and H6 in AtCAT5.

A, B Surface-rendered representation of AtCAT5 at 0 (A) and 450 ns (B) showing the opening of the cytoplasmic access tunnel. PPT molecule is presented as a red ball figure. C Protein contact atlas showing weighted interaction between PPT and specific AtCAT5 residues throughout the 450 ns simulation. Edge thickness represents interaction weight. Residues G272 and G273, emphasized in dark red, are selected based on the weighted interaction metrics, pocket location, and evolutionary conservation presented in Table S6 and Fig. S13. D, E Positional changes of helices H1 (blue), H3 (gray), H6 (red), and H8 (yellow) in AtCAT5 (D) and AtCAT5-G272W/G273W mutant (E). Structures at 450 ns (solid) are superimposed over their 0 ns counterparts (translucent). The directions of major rotational changes are indicated by black arrows and the corresponding angles provided. F Distance between helices within AtCAT5 and AtCAT5-G272W/G273W mutant. Values presented are the mean distances of the first and last 20 ns of the 450 ns simulation, with distance calculated as the mean of all pairs from two sets. Relevant data are presented in Fig. S13–S14. G Response of Tak-1, AtCAT5ox lines, and AtCAT5-G272W/G273Wox lines to PPT. Additional data presented in Fig. S15. Source data are provided as a Source Data file.