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![[Figure 7]](ji5027fig7mag.jpg)
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Figure 7
Superimposition of catalytic (α/β)8-barrel domains. (a) Superimposition of the catalytic (α/β)8-barrel domains of the alkaline α-galactosidase AtAkαGal3 (green), rice α-galactosidase (gray) and T. maritima α-galactosidase (yellow) with the product galactose at the respective −1 subsite. An extra loop (residues 329–352, magenta) exists exclusively in AtAkαGal3. (b) The complex of D383A with stachyose reveals that an extra loop helps to stabilize the product or stachyose substrate at the +2 and +3 subsites in the alkaline α-galactosidase AtAkαGal3. An electrostatic surface is shown (blue, positive charge; red, negative charge). (c, d) Docking of stachyose from the D383A complex into the structures of rice α-galactosidase (c) and T. maritima α-galactosidase (d) shows that both catalytic binding sites are shallow such that they can accommodate only one galactose, compared with AtAkαGal3 that can hold four-sugar moieties such as stachyose. |
![[Figure 7]](ji5027fig7.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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