Fig 5. The structural similarity between the nucleotide-binding pocket in MccE and the putative nucleotide-binding site in PseH.

The positions of the protein side-chains that form similar interactions with the nucleotide moiety of the substrate and with AcCoA are shown in a stick representation. The 3'-phosphate AMP moiety of CoA is omitted for clarity. (A) Key interactions between the protein and the nucleotide in the complex of the acetyltransferase domain of MccE with AcCoA and AMP. The protein backbone is shown as ribbon structure in light green for clarity of illustration. The AMP and AcCoA molecules are shown in ball-and-stick CPK representation and coloured according to atom type, with carbon atoms in black, nitrogen in blue, oxygen in red, phosphorus in magenta and sulphur in yellow. (B) The corresponding active-site residues in PseH and the docked model for the substrate UDP-4-amino-4,6-dideoxy-β-L-AltNAc. The protein backbone is shown as ribbon structure in light grey for clarity of illustration. AcCoA and modeled UDP-sugar are shown in ball-and-stick CPK representation and coloured according to atom type, with carbon atoms in black, nitrogen in blue, oxygen in red, phosphorus in magenta and sulphur in yellow.