Figure 2.
Figure 2: Nucleotide-dependent movements of the mechanical
elements of kinesin motors. a, Reorientation of the neck
linker between the ADP (yellow) and ATP-like (red) states of
KIF1A. b, Superposition of the switch II clusters of the
plus-end-directed kinesins. Conformation of the switch II
cluster (ADP or ATP-like, yellow and red, respectively) controls
position of the kinesin neck linker in all structures. Helix
6
is shown in blue. c, Hypothetical model for the
nucleotide-dependent dynamics at the core/neck interface of the
minus-end-directed motor ncd^9. The colours are the same as in a
and b. The switch II cluster and the neck in ATP state are
dashed. Conserved residues essential for stabilization of the
neck/core interface in the ADP state of the ncd^9 are labelled.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2001,
411,
439-445)
copyright 2001.
6
is shown in blue. c, Hypothetical model for the
nucleotide-dependent dynamics at the core/neck interface of the
minus-end-directed motor ncd^9. The colours are the same as in a
and b. The switch II cluster and the neck in ATP state are
dashed. Conserved residues essential for stabilization of the
neck/core interface in the ADP state of the ncd^9 are labelled.