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Figure 1.
FIG. 1. Conformations of the forms I (a and b), II (c and
d), and III (e and g) solved in this study. The upper row shows
the solved structures of the three forms. This is nominally the
front side of the enzyme. The amino-terminal  -sandwich (red),
catalytic core (blue), -barrel 1 (magenta), and
-barrel 2 (orange)
domains are shown. The Ca^2^+ ions are shown in yellow, the sole
Mg2^+ ion in cyan. Below are shown the electrostatic surface
potential images. The acidic and basic residues are colored red
and blue, respectively. The electrostatic potentials, including
Ca^2^+ and Mg2^+ ions, have been mapped onto the surface plan
from -15 kT (deep red) to +15 kT (deep blue). The open channel
is clearly evident in b. In g, the back side of the enzyme has a
deep cavity; the front side (f) remains closed.
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