Fig. 3

Comparative 3-D modeling of MIP-GFP and Wt-MIP proteins. 3-D protein models of Wt-MIP and MIP-GFP were created in PHYRE-2 [62]. Proteins are colored coded with Wt-MIP shown in (Blue) A MIP-GFP (Blue/Green) B Superimposed images [66] display Wt-MIP in (Blue) and MIP-GFP (Purple/Green), C MIP-GFP catalytic activity was compared to that of Wt-GFP, D Basak et al. [65] described six highly conserved amino acid patterns found in active sites of crystal structures from eukaryotes and prokaryotes. Four of the most highly conserved motifs are colored: HNVCEDSLL (Red), DSKVAMDEY (Orange), FRSKEISKS (Yellow), and YNHLGNNDG (Pink). Highly conserved amino acids, Ser323, Gly324, Gln325, Thr326, Lys369, Lys373, Lys412 and Lys489, are thought to be important for catalytic activity [65]. The local RMSD (root mean square deviation) for the two models, 1.61 Å, is < 2.0 Å, whereas the global RMSD, 3.65 Å, is > 2.0 Å. These RMSD values specify a conformational change with functional conservation [66]