Figure 2.
Figure 2. Binding of maltotriitol to the MBP closed form in
the C2 space group crystal. The sugar residues are labeled -G1
for the glucitol, followed by G1, G2, and G3 for the glucose
residues. (a) Difference (F[o] -F[c]) omit electron density map
(blue) at 2.3 Å resolution of the maltotriitol contoured
at 2s level. (b) Stereo view of the hydrogen bonds ( slant
3.4 Å) (broken lines) and stacking interactions between
the maltotriitol and MBP. With the exception of E111 and E153,
all the polar residues (blue color) that are involved in
hydrogen-bonding interactions originate from domain I. E111 and
E153 (red color) are located in domain II and the hinge
connecting the two domains, respectively. The aromatic residues
(colored green) originate from domain I (W62) and domain II
(W230, Y155, W340).
The above figure is reprinted
by permission from Elsevier:
J Mol Biol
(2001,
306,
1115-1126)
copyright 2001.
slant
3.4 Å) (broken lines) and stacking interactions between
the maltotriitol and MBP. With the exception of E111 and E153,
all the polar residues (blue color) that are involved in
hydrogen-bonding interactions originate from domain I. E111 and
E153 (red color) are located in domain II and the hinge
connecting the two domains, respectively. The aromatic residues
(colored green) originate from domain I (W62) and domain II
(W230, Y155, W340).