   2.4.1.102 | dimer |
the monomer units of the observed dimer C2GnT possesses the GT-A fold and are connected by a disulfide bond between the Cys235 residues, quantum mechanical/molecular modeling using enzyme crystal structures, PDB IDs 2GAK and 2GAM, as templates. The structure of C2GnT contains two regions; the first (38-121) is composed of alpha-helices. The second region, which corresponds to the catalytic domain (122-428), is an alpha/beta/alpha structure consisting of a central six-stranded mixed beta-sheet. Four disulfide bonds are found in each monomer (Cys151-Cys199, Cys372-Cys381, Cys59-Cys413, and Cys100-Cys172), the remaining Cys217 is unpaired and located in the donor binding site. C2GnT may occur in an open conformation, and a closed conformation. The location of the C2GnT-conserved Glu320 residue structurally corresponds to the catalytic base found in other glycosyltransferases with the GT-A fold |
735958 |
