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. 2012 Jun 28;7(6):e39297. doi: 10.1371/journal.pone.0039297

Figure 4. Superposition of modeled hTYW2 with the structure its archaeal homolog.

Figure 4

A) Superposition of the modeled hTYW2 (in beige) with the crystal structures of Pyrococcus horikoshii TYW2 in the AdoMet bound (PDB-ID:3A25, in green) and unbound (PDB-ID:3K6R, in cyan) forms is shown. The figure was created using PyMOL visualization software (www.pymol.org). The strands are displayed as arrows. The AdoMet is shown as a stick model colored in pink with nitrogen atoms in dark blue and oxygen atoms in red. The five amino acid residues in the AdoMet binding pocket of hTYW2 that were chosen for mutagenesis are labeled, and the H-bonds formed by these residues with AdoMet are shown in yellow dashed lines. B) A view of the AdoMet binding pocket with only AdoMet and the residues chosen for mutagenesis. AdoMet is shown as a stick with the atoms labeled. H-bonding interaction of the residues with AdoMet are indicated by dashed-lines: E265 with the O2* and O3* of the ribose moiety, D293 with N6 of the Adenine ring, and K225 with the terminal oxygen of AdoMet.