Figure 5 - full size

 

Figure 5.
Fig. 5. Structural comparison of MTG and FTG. A, overall structures; B, structures around the active sites of MTG (left) and FTG (right). The top views of MTG are drawn with a green ribbon model. The four domains of FTG ( -sandwich, core, barrel 1, and barrel 2) are shown in light blue, dark blue, light purple, and dark purple, respectively. The catalytic triad of FTG (Cys272, His332, and Asp355) and the positionally corresponding residues of MTG (Cys64, Asp255, and His274) are represented by the red wire model. These illustrations were drawn using the program QUANTA (Molecular Simulation Inc.). In A, the regions enclosed by yellow circles, a green circle, and a purple circle represent active sites, a possible acyl donor binding site of FTG, and a possible acyl acceptor binding site of FTG, respectively. C, stereo view of the superposition of the active site of MTG (green) on those of FTG (light blue). The catalytic triads of FTG and MTG, as well as the residues (S293(MTG) and Y515(FTG)) in which the side chains interact with the side chains of the catalytic triads (H274(MTG) and C272(FTG), respectively), are represented. The ball-and-stick representations were drawn using the program MOLSCRIPT.

The above figure is reprinted by permission from the ASBMB: J Biol Chem (2002, 277, 44252-44260) copyright 2002.