 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
journal menu
![[Figure 3]](wd5068fig3mag.jpg)
|
|
Figure 3
(a) Three-dimensional representation of a hypothetical model of the intact trilobed protease. Structure prediction of the α/β-hydrolase domain was performed using the LIBELLULA server (Juan et al., 2003  ) and is shown in brown. The β-propeller domain is depicted as in the previous figures. Both domains were fitted using the program TOP (Lu, 2000) according to the overall structure of prolyl oligopeptidase (Fülöp et al., 1998). Residues of the active site are shown as green spheres. (b) Schematic overview of possible substrate pathways in the monomeric trilobed enzyme. Green arrows represent substrate access to the active site; the catalytic domain is represented as a cone-shaped domain and the β-propeller domain is colour coded by individual blades. The first model represents a diffuse only model, where the pore cannot be widened, and the second model allows a limited widening of the central pore; both cases are applicable to the Velcro-type closures of β-propeller domains. The third and the fourth model result in larger movements of the β-propeller domain and are limited to non-Velcro-type β-propellers, allowing a larger breathing mechanism for the uptake of larger substrates. The last model is a combination of the breathing mechanism and an additional domain movement, allowing much larger substrates to access the catalytic site via the side entrance. |
![[Figure 3]](wd5068fig3.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
