Figure 8 | Scientific Reports

Figure 8

From: Two novel fish paralogs provide insights into the Rid family of imine deaminases active in pre-empting enamine/imine metabolic damage

Figure 8

Crystal structures of SsRidA-1 and SsRidA-2. (A) Ribbon representation of the SsRidA-1 trimer. (B) Ribbon representation of the SsRidA-2 trimer. (C) Stick representation of β1 and β2 strands of SsRidA-1 and SsRidA-2 in cyan and orange, respectively. H-bonds are shown as dashed lines. In SsRidA-2, the presence of Pro9 shortens β1 strand and reduces the H-bond network. (D) Stick representation of β1 and β9 strands of the adjacent monomer present in the SsRidA-1 trimer. (E) Superposition of SsRidA-1 and SsRidA-2 monomers color-coded as in C. (F) Zoom on the active site cavity of SsRidA-1(left) and SsRidA-2 (right) shown as surface colored according to the electrostatic potential. SsRidA-2 clearly displays a stronger electropositive cavity than SsRidA-1. Acetate molecules (in green) present in the active site of both salmon RidA isoforms and the sulphate ion (in yellow) present in SsRidA-2 are shown in sticks. (G) Stereo-view of the SsRidA-1 and SsRidA-2 active sites, color-coded as in C.

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