Figure 2.
Figure 2: Nucleotide-binding site and distortion of the
beta--sheet
at the interface of the N-terminal and upper 50-kDa subdomains.
a, Shown is an overlay of the -sheet
(N-terminal subdomain superimposed) between myosin V in blue and
near rigor (Dictyostelium myosin II) in grey. Note that strands
5 -7, which belong to the upper 50-kDa subdomain are distorted
to allow the upper 50-kDa rotation that removes switch I from
the nucleotide-binding site. b, The positions of the
nucleotide-binding elements are shown for three myosin states.
The yellow asterisk in the myosin V structure marks the position
of the Mg2+ in the other structures. In the transition state,
switch II contributes to coordination of the -phosphate
of the nucleotide, but it bends in myosin V in the opposite
direction and forms direct interactions (broken green lines)
with the fourth -strand
and the P loop of the N-terminal subdomain.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2003,
425,
419-423)
copyright 2003.
-sheet
at the interface of the N-terminal and upper 50-kDa subdomains.
a, Shown is an overlay of the 
-sheet
(N-terminal subdomain superimposed) between myosin V in blue and
near rigor (Dictyostelium myosin II) in grey. Note that strands
5 -7, which belong to the upper 50-kDa subdomain are distorted
to allow the upper 50-kDa rotation that removes switch I from
the nucleotide-binding site. b, The positions of the
nucleotide-binding elements are shown for three myosin states.
The yellow asterisk in the myosin V structure marks the position
of the Mg2+ in the other structures. In the transition state,
switch II contributes to coordination of the 
-phosphate
of the nucleotide, but it bends in myosin V in the opposite
direction and forms direct interactions (broken green lines)
with the fourth