Figure 3: Structural views of mono-functional and bi-functional GalE from different organisms.

(A) The predicted structure of GalE from N. meningitidis MC58 obtained using PHYRE2. The structure is depicted as a ribbon representation showing the secondary structure elements. The side chains for residues which are not conserved amongst all neisseria species are shown in stick representation. Position 300 in N. gonorrhoeae strain FA1090 is labelled. (B) The active site region of GalE from E. coli in complex with NADH and UDP-GlcNAc (PDB code 1LRJ)¹⁷. The protein alpha carbon trace is shown. The bound ligands and side chains for residues involved in interaction with the bound ligands are indicated by stick representation. A mesh surface is shown for Tyr299. (C) The active site region of GalE from H. sapiens in complex with NADH and UDP-GlcNAc (PDB code 1HZJ)¹⁷. The bound ligands and side chains for residues involved in interaction with the bound ligands are indicated by stick representation. A mesh surface is shown for Cys307. (D) The active site region of the PHYRE2 predicted structure of GalE from N. meningitidis MC58. The conserved side chains for residues implicated in interaction with the substrates are indicated by stick representation. A mesh surface is shown for Phe300. (F) The active site region of the PHYRE2 predicted structure of GalE from N. gonorrhoeae FA1090. The conserved side chains for residues implicated in interaction with the substrates are indicated by stick representation. A mesh surface is shown for Ser299.