FIGURE 1.

Crystal structure of sPOMGNT2 and its interaction with UDP. (a) Overall structure of the sPOMGN2 dimer. Each monomer is colored green and pale blue, and bound UDP molecules are shown in stick models. (b) Domain structure of the monomer. The N‐terminal catalytic domain consists of an N‐lobe (residues 53–277, blue) and C‐lobe (residues 286–476, green). The C‐terminal FnIII domain (residues 477–580) is colored orange. (c) Interaction between sPOMGNT2 and UDP. Side chains of the residues which interact with UDP are shown by stick models colored blue (N‐lobe) and green (C‐lobe). UDP is shown by a gray and orange stick model. Red dotted lines are hydrogen bonds. (d, left) Enzymatic activities of the WT and N163A mutant of sPOMGNT2. sPOMGNT2 immunoprecipitated from the cell lysate was used because the N163A mutant was scarcely secreted to the culture media. (d, right) Enzymatic activities of the WT, R294A, and R298A mutants of sPOMGNT2. sPOMGNT2 immunoprecipitated from the culture media was used. Insets: immunoblot analyses of sPOMGNT2 proteins to normalize input sPOMGNT2. ND means that the activities were not detected. Average values ± SE of three independent experiments are shown