Figure 4.
Figure 4 The activation of EF and CyaA-N by wild-type CaM and
two series of CaM mutants. EF (1 nM) and CyaA-N (0.7 nM) were
used for an adenylyl cyclase activity assay in the presence of
0.1 M
free Ca^2+ with CaM mutants CaM 41/75 and 85/112. Each mutant
has two cysteine mutations to lock either the N- or the
C-terminal domain of CaM in the closed conformation (A and B).
The same concentrations of EF and CyaA-N were used for an
adenylyl cyclase activity assay in the presence of 1 M
free Ca^2+ with CaM mutants B1Q, B2Q, B3Q and B4Q. Each mutant
has a mutation inactivating one of four calcium-binding sites (C
and D). Means SE
are representative of at least two experiments.
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2002,
21,
6721-6732)
copyright 2002.
M
free Ca^2+ with CaM mutants CaM 41/75 and 85/112. Each mutant
has two cysteine mutations to lock either the N- or the
C-terminal domain of CaM in the closed conformation (A and B).
The same concentrations of EF and CyaA-N were used for an
adenylyl cyclase activity assay in the presence of 1 
SE
are representative of at least two experiments.