Figure 6.

Visualization of conformational differences in the open and closed conformer of NbUGT72AY1.

(A) Distance of Nε2-His to OH-scopoletin, Nδ1-His to COOH-Asp, and OH-scopoletin to C1-UDP-Glc in the ternary complex (NbUGT72AY1•scopoletin•UDP-Glc); HDX results with scopoletin/UDP are color-mapped, and the open conformer is shown.

(B) Same as in (A), but the closed conformer is shown.

(C) UDP-Glc binding pocket, showing the rotation of Trp350; HDX results with scopoletin/UDP are color-mapped, and the open conformer is shown.

(D) Same as in (C), but the closed conformer is shown.

(E) Putative allosteric binding site formed after rotation of Arg91; HDX results with scopoletin/HDX are color-mapped, and the open conformer is shown.

(F) Same as in (E), but the closed conformer is shown.

(G) Surface presentation of the open conformation of NbUGT72AY1; HDX results with scopoletin/UDP are color-mapped. Red circle shows the putative allosteric site, which is closed in the open conformer.

(H) Surface presentation of the closed conformation of NbUGT72AY1. The new binding site is marked by a red circle.

(I) Same as in (H), with scopoletin bound in the putative allosteric binding site.

(J) Phe120 is located between the catalytic and allosteric sites.