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Figure 4.
FIG. 4. Acyclic form of FBP docked in the active site and
superposition with MBP bound structure. The ketohexose-P[2] was
docked manually by superposition onto the determined MBP
structure, shown in Fig. 3A. The modeled structure was then
subjected to 2000 steps of conjugated gradient minimization with
CNS using topology and parameters from PRODRG. Hydrogen bonding
patterns (green dashes) were conserved when compared with those
in FBP and MBP enzyme adducts. The only significant difference
with respect to the observed enzyme adducts is an additional
hydrogen bond made by Glu-187 with FBP O[2]. The orange dash
illustrates the putative nucleophilic face si attack made on FBP
C[2] carbonyl by Lys-229. Orientation is similar to Fig. 1.
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