Supporting Figures

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Fig. 5. Sequence alignments and schematic representations of repeats in (A) TcdA and (B) TcdB (strain VPI 10463). In the sequence alignments, positions in the repeats where the structure of TcdA-f1 indicates a structural reason for a high degree of sequence conservation are highlighted by shading and coloring. The conserved tyrosine and aspartate/histidine residues in the short repeat (SR) preceding each long repeat (LR) are colored yellow and green, respectively. In the schematic diagrams, SRs are represented by light blue boxes, whereas LRs are represented by dark blue boxes.

Fig. 6. (A) Structure-based sequence alignment of TcdA-f1 with pneumococcal autolysin [Protein Data Bank (PDB) ID code 1GVM] and phage endolysin (PDB ID code 1H09) cell-wall-binding repeats (least-squares superpositions of Ca atoms were performed by using lsqman). * represents an aligned residue between TcdA-f1 and autolysin (top *) or endolysin (bottom *). b-strand assignments from dssp are represented by green arrows. Stereoscopic views of superpositions of TcdA-f1 (gray) with (B) autolysin (red) and (C) endolysin (magenta): rms deviation (rmsd) 1.61 Å for 76 residues aligned. (D) Stereoscopic view of the choline-binding pockets in autolysin (red) and endolysin (magenta), superimposed on the equivalent structure in TcdA (gray). A ribbon representation of the backbone and a stick representation of the aromatic side chains forming the pocket are drawn. A choline molecule from the autolysin complex structure is drawn in space-filling representation.