EC Number   |
|---|
   2.4.1.B62 | catalytic fragment of toxin B in the presence of UDP-glucose and Mn2+, to 2.2 A resolution. Toxin B belongs to the glycosyltransferase type A family. The reaction proceeds probably along a single-displacement pathway. The C1'' donor carbon atom position is defined by the bound UDP and glucose. The relative orientation of toxin B and substrate RhoA is consistent with both being attached to a membrane |
| 2.4.1.B62 | catalytic fragment, residues 1-546, to 2.3 A resolution. Geometry suggests that the reaction runs as a circular electron transfer in a six-membered ring, which involves the deprotonation of the nucleophile by the beta-phosphoryl group of the donor substrate UDP-glucose |
| 2.4.1.B62 | catalytic fragment, residues 1-551 to 2.85 A resolution. Geometry suggests that the reaction runs as a circular electron transfer in a six-membered ring, which involves the deprotonation of the nucleophile by the beta-phosphoryl group of the donor substrate UDP-glucose |
| 2.4.1.B62 | crystal structures of the toxin A glucosyltransferase domain in the presence and absence of the co-substrate UDP-alpha-D-glucose, to 2.2 and 2.6 A resolution, respectively |
| 2.4.1.B62 | enzyme contains an internal cysteine protease domain allosterically regulated by the eukaryotic-specific molecule inositol hexakisphosphate. Apo-cysteine protease is in dynamic equilibrium between active and inactive states. Inositol hexakisphosphate dramatically shifts this equilibrium towards an active conformer that is further restrained upon binding a suicide substrate. Residues within a beta-hairpin region functionally couple the inositol hexakisphosphate binding site to the active site |
