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Figure 5.
FIG. 5. The active site architecture of AguA. a, stereo
view of the E285N-substrate complex (red) superimposed with the
WT-products complex (green), showing the hydrogen bonds (dotted
lines) and distances between the catalytic residues, the
nucleophilic water and the substrate/products. The inset on the
right shows the two different conformations of the MeGlcA sugar
ring in the two complexes. b, a superposition of the E386Q
mutant active site (purple), the active site of the WT AguA in
complex with the reaction products MeGlcA and xylotriose
(green), and the free WT enzyme (cyan), demonstrating the
conformational flexibility and movement of the 283-287 loop
following substrate binding and catalysis. The relevant parts of
WT AguA confirm that it is practically identical to the E386Q
mutant.
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