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Figure 3.
Figure 3. The Open Conformation of the Nucleotide Binding
Pocket of KIF2C in the AMP-PNP Form(A) Comparison of the
structures of KIF2C in the ADP form (red) and in the AMP-PNP
form (blue). The interaction between the neck (green) and the
KVD-finger (pink) is also shown. Note the disulfide bond
(yellow) between the neck and the KVD-finger.(B) Comparison of
the configuration of the switch I and switch II regions of KIF1A
(purple) and KIF2C (blue). Although both structures are of the
AMP-PXP (X = C or N) form, the switch I loop is distant from the
γ-phosphate due to the rotation of α3. To move the switch I
loop closer to the γ-phosphate, α3 must be rotated as shown by
the yellow arrows. This rotation may be triggered by the
preceding L8 loop. This open conformation of the switch I loop
is similar to the structure of the salt bridge mutant (R598A) of
Kar3. The structures of the wild-type (purple) and R598A mutant
(blue) of Kar3 are shown for comparison (C). The mutation
resulted in the rotation of α3 and the switch I loop moved away
from the nucleotide binding pocket (yellow arrow).
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