Figure 4 - full size

 

Figure 4.
Fig. 4. Binding of FAD to MICAL[fd].(A) Electron density of the bound FAD. The SigmaA-weighted map was calculated by using 2mF[o]-DF[c] coefficients (45). Some of the protein residues contacting the FAD are shown. (B) Stereoview of the interactions of FAD with MICAL[fd] residues. The following coloring scheme was used for the protein atoms: C, cyan; N, blue; O, red. Water molecules are represented by red spheres. Colors used for the FAD differ only in that carbons are green and phosphates are magenta. (C) Two bound conformations of FAD. The surface of the protein in the cavity around the FAD is shown as an electrostatic surface. The protein atoms surrounding the cavity are shown with carbons colored green, nitrogens colored blue, and oxygens colored orange. The same colors are used for the FAD in the "out" conformation (crystal) with the addition of magenta for phosphorous. The portion of the FAD that has moved in the "in" conformation (model) has yellow carbon atoms.