FIGURE 1.

Structure of fascin and amino acids mutated in this study. Wall-eyed stereo diagram of the 2.0-Å-resolution crystal structure of fascin, showing ribbon and surface representations. There are two fascin molecules in the asymmetric unit of the crystal; only molecule A is shown. The four β-trefoil domains are highlighted with different colors as indicated by the diagram at the bottom of the figure. Also shown are the side chains of residues mutated in this study (cyan), molecules of glycerol and PEG bound in the structure, and Ser³⁹ (red), which is phosphorylated by PKC. Note that a large groove effectively separates the four β-trefoil domains into two pairs, 1-2 and 3-4. Inter-β-trefoil domain contacts are more extensive within pairs (see also supplemental Fig. 1 and supplemental Movie 1). N-ter, N terminus; C-ter, C terminus.