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Figure 4.
Fig. 4. Structure of the GS-1-complexed actin trimer.
Actin subunits in the trimer complex are colored in dark green,
orange, and blue. The corresponding segments of gelsolin are
light green, yellow, and cyan. The structure of each GS-1-bound
protomer in the trimer is similar to the structures of
GS-1-complexed actin solved previously. In each protomer, the
bound nucleotide, Ca^2+-ATP, is shown as a gray space-filling
model. Coordinated ions of Ca^2+ are drawn as red spheres. The
pPDM cross-link is between Lys-193 of one actin subunit and
Cys-376 of its neighbor. In each actin subunit, the C-terminal
residues 375-377 and residues corresponding to DNase I binding
loop are disordered and are not included in the model. The
dashed lines, therefore, connect the cross-linked Lys-193 of
subunits 1 and 2 to the last visible C-terminal residue,
Arg-374, of subunits 2 and 3, respectively.
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