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Figure 5.
Fig. 5. Structural comparison of substrate binding sites
of AANAT , tGCN5, and GNA1. The molecular surfaces around the
active site of the AANAT-bisubstrate analog (A), the
tGCN5-CoA-H3peptide (B), and the GNA1-CoA-GlcNAc6P complex
structures (C) are viewed with a similar orientation. From top
to bottom, the serotonin-like moiety and the acetyl group are
shown in red, the H3 peptide backbone in yellow, with its
reactive Lys-14 side chain in orange, and GlcNAc6P in purple.
Structural divergences within the NH[2]- and COOH-terminal
regions are highlighted in dark blue and blue, respectively. The
 3- 4 insertion
loop unique to AANAT is shown in brown.
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