Extended Data Fig. 6: Dynamic Conformation of Sgt2 Chaperoning Complex with TA Clients.
From: Remote on–off switching of protein activity by intrinsically disordered region
a, Far-UV CD spectra of Sgt2C (left) and Sgt2C-Ysy6TMD (right) in 5% (blue) and 10% TFE (green). TFE induces increased helical content in Sgt2C and Sgt2C-Ysy6TMD. b, 1H-15N HSQC spectra overlay of Sgt2C-Ysy6TMD under native conditions (Modena) and 10% TFE (azure). Presence of TFE enhances structural stability but fails to eliminate the high dynamic nature of the Sgt2C-Ysy6TMD complex, evidenced by missing signals. c, NMR characterization of various chaperoning complex fusion constructs (top cartoons) displayed in 1H-15N HSQC NMR spectra, revealing broadened signals with poor dispersion, characteristic of a molten-globule-like conformation. Structural instability persists despite changes in fusion orientation or Sgt2C supply. d, SAXS analysis of Ysy6TMD-loaded Sgt2 confirming the structural flexibility of the complex.
