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Figure 3.
Figure 3: Active site of BluB. a, b, The active site with
oxidized FMN (a) and reduced FMN (b), viewed from the re-face.
H-bonds are represented as dashed lines. For clarity, water
molecules are not rendered in this view. The rearrangement in
H-bonds around N1 reflects the change in protonation in the
reduced structure. Asp 32 may also form a close contact with C1'
of the ribityl chain, suggesting a potential catalytic role for
this residue. c, d, Side views of the active site in the
oxidized (c) and reduced (d) structures. For clarity, Arg 34 has
not been rendered in this view. The sigma-A weighted 2F[o]-F[c]
electron density map is contoured at 1  and
coloured grey (around protein side chains), blue (around
FMN/FMNH[2]) and red (around water/oxygen) to enhance contrast.
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