Extended Data Fig. 5: Structural alignment of GalS1 with mammalian β-GlcNAc β-1,4-galactosyltransferases (β4GalTs).
From: Structural and biochemical insight into a modular β-1,4-galactan synthase in plants
The core catalytic domain of GalS1 (ivory) is well aligned with other galactosyltransferases (differently colored). GalS1 shows additional N- and C-terminal domains that are hypothesized to be necessary for binding the RG-I backbone to facilitate galactan chain elongation. GalS1 is aligned with a, Bos taurus Btβ4GalT1 (RMSD 4.7 over 104 residues, green);53 b, Homo sapiens Hsβ4GalT7 (RSMD 5.6 over 128 residues, magenta);35 c, Homo sapiens Hsβ4GalT1 (RMSD 4.2 over 104 residues, aqua);54 and d, Drosophila melanogaster Dmβ4GalT7 and (RMSD 5.7 over 136 residues, red)35.
