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Figure 3.
Figure 3 Cleft closure. (A) The lower and upper 50 kDa
subdomains of myosin V MDE have been pulled apart exposing the
surface interactions allowing cleft closure. Note (in green on
the right) the U50 highly conserved linker that interacts with
the HW and HP helices (white on the left) of the L50 subdomain.
Switch II (orange) and the strut (pink) are two connectors
between the subdomains that help mediate the interactions
between these two surfaces and they are shown on both sides. In
particular, a hydrophobic residue of switch II (Y439, yellow
ball and stick) is a serine or alanine in all myosin II
isoforms. This difference may account in part for the difference
in the kinetics of cleft closure for the two molecules. (B) A
surface CPK representation of the residues involved in this
interface is presented in the same orientation as in A).
Depending on the conservation in the sequence of these residues
in the myosin superfamily, different colors are used (absolutely
conserved (green), conservative changes (pale green) and
nonconserved (purple)). A yellow star indicates how to
reposition the two surfaces to reconstruct the interface.
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