Extended Data Fig. 2: Disordered Conformation of Sgt2’s C-Terminal Tail.
From: Remote on–off switching of protein activity by intrinsically disordered region
a, 1H-15N HSQC NMR spectra of Sgt2C, revealing a lack of signal dispersion indicative of a disordered conformation, with assignments labeled. b, 1H-13C HMQC NMR spectra of Sgt2C, displaying limited signal dispersion consistent with a disordered conformation, with assignments labeled. c, Far-UV circular dichroism (CD) thermal denaturation of Sgt2C showing a prolonged transition, suggesting a non-cooperative unfolding process. d, Prediction of intrinsic disorder in Sgt2 using Metadisorder (top) and IUpred3 programs (bottom). In the Metadisorder plot, different colors indicate predictions from various methods: MetaDisorder3D (purple) uses structural alignments, MetaDisorder (blue) is a consensus-based predictor, MetaDisorderMD (green) integrates sequence- and structure-based predictions, and MetaDisorderMD2 (red) further optimizes these predictions. Both programs identify the C-terminal tail and the linker connecting Sgt2N and Sgt2T are disordered. e, Superposition of the 20 lowest-energy solution structures of Sgt2 with the Sgt2N domains aligned, revealing a highly dynamic “beads-on-string” conformation with minimal additional interdomain contacts beyond the N-domain dimerization. The color scheme for Sgt2’s domains is consistent with the schematic representation at the top. The inset highlights the well-aligned 20 structures of Sgt2N.
