|
Figure 3.
Fig. 3. Structure alignment of N-CaM with N-terminal domain
of the NMR structure of apo-CaM (left, 1CFD) and the X-ray
structure of Ca^2+-CaM (right, 1CLL). The residues involved in
ion coordination are shown as sticks and labeled. These global
alignments were performed using helices A and D, and show that
our structure is predominantly in the closed conformation. 1CFD
and 1CLL are presented as transparent. The two
helix–loop–helix EF-hand Zn^2+-binding sites are shown in
different colors: EF-hand I (helices A and B), rose red; EF-hand
II (helices C and D), lime green. The spheres show the two Zn^2+
ions present in these binding sites. The zinc ion in site 2 has
double occupancy. There is also a cacodylate molecule present
from the crystal growth buffer with arsenic shown in purple.
|