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).
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2006,
281,
9623-9632)
copyright 2006.
-carbon
of Ile-223 and the heme iron atom from 6.7 Å (bsNOS) to
6.1 Å (gsNOS).