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. 2015 Mar 17;10(3):e0115634. doi: 10.1371/journal.pone.0115634

Fig 3. Comparisons of PseH with other GNAT superfamily enzymes.

Fig 3

(A) Stereo ribbon diagram of the superimposed structures of PseH from H. pylori (black), RimL from S. typhimurium (red) and the acetyltransferase domain of MccE from E. coli (green). The side chains of the conserved tyrosine in PseH and serine in MccE and RimL, likely to be implicated in deprotonation of the leaving thiolate anion of CoA in the reaction, are shown using a stick representation. (B) A sequence alignment of PseH, RimL, MccE and WecD from E. coli. The elements of the secondary structure and the sequence numbering for PseH are shown above the alignment. Conserved residues are highlighted in red. (C) Comparison of dimers observed in the crystal structures of PseH (in which the two halves of the dimer are drawn in black and grey) and RimL (red/salmon). (D) Comparison of the structures of PseH and WecD. Like PseH, WecD catalyses transfer of an acetyl group from AcCoA to the 4-amino moiety of the nucleotide-linked sugar substrate. Structurally equivalent domains are drawn in the same colour. The additional N-terminal domain in WecD is shown in yellow.