journal menu
![[Figure 1]](ji5027fig1mag.jpg)
|
|
Figure 1
Active site of the crystal structure of AtAkαGal3. (a) The crystal structure of wild-type AtAkαGal3. The detailed interactions of galactose (yellow sticks) in a β-anomeric form with residues (yellow sticks) at the −1 subsite are shown. OH1 of galactose makes a hydrogen-bond interaction with the side chain of Asp383 and a water molecule (cyan sphere), with distances of 3.06 and 2.66 Å, respectively. Three water molecules (cyan spheres) help to stabilize the galactose moiety through water-mediated hydrogen-bonding interactions with Trp78, Lys381, Arg443, Asp447 and Asp479. (b) A galactose bound at the catalytic site of the D383A mutant forms an interaction network with residues similar to that in wild-type AtAkαGal3, except that there is a direct interaction between OD2 of Asp447 and O1 of the galactose moiety; two additional water molecules (cyan spheres) help to stabilize O1 and O6 of galactose as Asp383 is replaced by alanine. |
![[Figure 1]](ji5027fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
Open 
access
access
