Fig. 1: The conformational change of SBPs and the evolution of PaCDT. | Nature Communications

Fig. 1: The conformational change of SBPs and the evolution of PaCDT.

From: Altered conformational sampling along an evolutionary trajectory changes the catalytic activity of an enzyme

Fig. 1

a X-ray crystal structures of SBPs that are specialised for binding solutes, such as AncCDT-1 (shown), typically capture open ligand-free (left, PDB 5TUJ) and closed liganded (right, PDB 5T0W) states. b Schematic drawing (not to scale) of the phylogenetic tree used for ancestral sequence reconstruction in Clifton et al.40, which highlights the evolutionary relationship between the polar amino acid-binding proteins (e.g., Thermotoga maritima L-arginine-binding protein, TmArgBP), AncCDT-1, AncCDT-3, AncCDT-5 and PaCDT. Clades are collapsed. Figure adapted from Clifton et al.40.

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