Figure 2.
FIGURE 2. Comparison of fused ring substrate binding in
SULT1A1, mouse SULT1E1, and human SULT2A1. A, stereoview of E2
binding in the SULT1A1 active site. The noncatalytic substrate
binding mode of SULT1A1 is shown in orange. The O-3 hydroxyl of
E2 can form hydrogen bonds (dotted lines) to PAP and Lys48 (not
shown for clarity). The proposed E2 catalytic orientation
(green) was modeled using GOLD. For comparison, the E2 binding
mode from mouse SULT1E1 is shown (light blue). B,
superimposition of C traces of
SULT1A1·PAP·pNP (pink) and
SULT1A1·PAP·E2 (green). E2 is shown in orange. A
loop (residues 84-90) that moves to accommodate E2 in the active
site is highlighted in dark blue and indicated by an arrow.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2005,
280,
41482-41486)
copyright 2005.
traces of
SULT1A1·PAP·pNP (pink) and
SULT1A1·PAP·E2 (green). E2 is shown in orange. A
loop (residues 84-90) that moves to accommodate E2 in the active
site is highlighted in dark blue and indicated by an arrow.