<p>(<b>A</b>) Primary structure of <i>C. reinhardtii</i> prePDS protein showing plastid transit peptide, dinucleotide binding Rossmann-like domain, and amino acid substitutions affecting PDS function (see Fig. 8). The same colour coding is used throughout <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0099894#pone-0099894-g007" target="_blank">Figs 7</a> and <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0099894#pone-0099894-g008" target="_blank">8</a>. (<b>B</b>) Ribbon representation of the predicted three-dimensional structure of <i>C. reinhardtii</i> PDS. Left: Phyre-based 3DLigandSite model; middle: Modeller-based BioSerf predicted structure; right: SwissModel predicted structure. Amino acids shown in A are indicated. The conserved Rossmann-like domain is shown as a yellow ribbon. (<b>C</b>) Residues in the predicted FAD-binding domain. Amino acids in the Rossmann-like domain are shaded yellow. Amino acids conferring norflurazon resistance lie adjacent to (F131/red, L505/green) or are part of the predicted domain (V472/pink). (<b>D</b>) 3D structure of the predicted FAD-binding region. Bound FAD is shown in the centre of the structure as a ball stick model. Yellow atoms are part of the Rossmann-like domain. F131, R268, V472, L505 and L517 are shown.</p
