|
Figure 4.
Figure 4. A schematic representation of the hydrogen
bonding networks of (a) the wild-type enzyme in the attack by a
catalytic water molecule on the C1 atom of Glc( -1) from above,
and (b) the wild-type enzyme after the inversion at the O1 atom.
Note that the Thr342 residue assumes different conformations in
(a) and (b). (c) The hydrogen bonding network rearranged in the
E380Q/maltose structure. The catalytic water molecule was
eliminated and a new water molecule was introduced between
Gln380 and Asn340. No interaction between Gln380 and Lys295 was
observed.
|
