FIGURE 3.

Structural and dynamic properties of the wild-type and mutant Ubl domains of SAE2. a, comparison of the secondary structures of the SAE2 Ubl domain estimated from NMR chemical shifts of the wild type (WT) (major and minor conformations), GGG insertion mutant, and 484Δ deletion mutant. The secondary structures in the x-ray crystal structure of the full-length protein are also shown. The cylinders and arrows represent helices and β-strands, respectively. The E2-binding regions were estimated through comparison with the NEDD8 structure and confirmed by NMR chemical shift perturbation (Fig. 2). b, ¹H-¹⁵N NOE of the wild-type and mutant SAE2 Ubl domains versus the residue number. Blue diamonds, major conformation; magenta squares, minor conformation. The secondary structures are shown at the top. The region that undergoes folding-unfolding equilibrium in the wild-type protein is highlighted.