Figure 8 - full size


Figure 8.
Fig. 8. pair comparing the posi- tions of side chains, metals, andphos- phate in the active sites of the D369N enzyme (thick lines) and the wild-type enzyme (thin lines). At the I site, zinc is bound close to he same location in both enzymes (crosses), but phosphate (PO,) is more exposed to the surface in the D369N structure. At the M2 site, zinc is bound n the wild-type (cross) but not theutant enzyme. This permits SI02 to move slightly closer to H370 and the asparagineintroduce at position 369 (D369N). The M3 site normally contains Mgz+ (cross) with 3 water molecules (not shown) in the wild-type enzyme; in the mutant enzyme this space is partially filled y 1 water molecule (not shown), the carboxylate side chain of D5 1, and the#-aminogroup of K328. The 2 sets of atomiccordinates were aligned using Quanta to minimize the RMSD of the Cor atomsbefore making this omparison.

The above figure is reprinted from an Open Access publication published by the Protein Society: Protein Sci (1994, 3, 2005-2014) copyright 1994.