Figure 5.
Figure 5. Structurally implied active site chemistry for
pure HhH glycosylase MIG. MIG interactions of Glu42 and Tyr126
with the O4, N3 and O2 positions of thymine facilitate
glycosylic bond dissociation, while the vert,
similar 90° clockwise twist and distortion enforced by the
MIG thymine-binding pocket allows the three normally orthogonal
O4', N-C1', and p electron orbitals to overlap. This orbital
overlap facilitates catalysis by promoting the electron
transpositions needed for glycosylic bond cleavage[16].
The above figure is reprinted
by permission from Elsevier:
J Mol Biol
(2002,
315,
373-384)
copyright 2002.
vert,
similar 90° clockwise twist and distortion enforced by the
MIG thymine-binding pocket allows the three normally orthogonal
O4', N-C1', and p electron orbitals to overlap. This orbital
overlap facilitates catalysis by promoting the electron
transpositions needed for glycosylic bond cleavage[16].