Divergence of AMP Deaminase in the Ice Worm Mesenchytraeus solifugus (Annelida, Clitellata, Enchytraeidae)

Figure 4

Four sterically constraining residues (K173, Y174, D444 and D445) define the surface area of the AMPD substrate binding plane as ~38   Å  2 in A. thaliana (a), ~36   Å 2 in A. thaliana K188E (b), ~36  Å  2 in the ice worm E188 (c), and predicted loss of structure in ice worm E188K (d). Position 188 is visible to the right in each panel.

(a)

(b)

(c)

(d)