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Figure 9.
FIGURE 9. Comparison of the active sites of bsNOS (orange)
and gsNOS (yellow). In bsNOS, Lys-356 does not interact with
Asp-216. A Lys to Arg substitution in gsNOS allows Arg-365 to
hydrogen bond with Asp-225 (3.2 Å), altering its side
chain position. This change in structure appears to be
correlated with movement of Ser-224 that in turn pushes Ile-223
into the active site, reducing the distance between the  -carbon
of Ile-223 and the heme iron atom from 6.7 Å (bsNOS) to
6.1 Å (gsNOS).
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