Figure 8 - full size


Figure 8.
FIG. 8. A, the view of modeled interactions of SQQ*VT (from loricrin) for the Gln* substrate and KTKQK* (from small proline-rich protein 1) as the Lys* substrate with GDP molecules that is shown in ball-and-stick. The side chains for the active site residues and Cys272, His330, and Asp353 are shown as ball-and-stick. B, the amino acid sequence alignment of TGases family is shown around the guanine nucleotide-binding site pocket. The amino acids highlighted in red are acidic, blue are basic, yellow are nonpolar, and green are polar residues. Arrows indicate the position of the Arg/Phe residues that stack over the guanine ring in TGase 2 and TGase 3 structures, respectively. The other arrows represent two basic residues that are essential for stabilizing the transition states for GTP hydrolysis.

The above figure is reprinted by permission from the ASBMB: J Biol Chem (2004, 279, 7180-7192) copyright 2004.