Three bacterial pectate lyases, a pectin lyase fromAspergillus niger,the structures of rhamnogalacturonase A fromAspergillus aculeatus,RGase A, and the P22-phage tailspike protein, TSP, display the right-handed parallel β-helix architecture first seen in pectate lyase. The lyases have 7 complete coils while RGase A and TSP have 11 and 12, respectively. Each coil contains three β-strands and three turn regions named PB1, T1, PB2, T2, PB3, and T3 in their order of occurrence. The lyases have homologous sequences but RGase A and TSP do not show obvious sequence homology either to the lyases or to each other. However, the structural similarities between all these molecules are so extensive that divergence from a common ancestor is much more probable than convergence to the same fold. The region PB2-T2-PB3 is the best conserved region in the lyases and shows the clearest structural similarity. Not only is the pleating and the direction of the hydrogen bonding in the sheets conserved, but so is the unusual αL-conformation turn between the two sheets. However, the overall shape, the position of long loops, a conserved α-helix that covers the amino-terminal end of the parallel β-helix and stacks of residues in αR-conformation at the start of PB1 all suggest a common ancestor. The functional similarity, that the enzymes all bind α-galactose containing polymers at an equivalent site involving PB1 and its two flanking turn regions, further supports divergent evolution. We suggest that the stacking of the coils and the unusual near perpendicular junction of PB2 and PB3 make the parallel β-helix fold especially likely to maintain similar main chain conformations during divergent evolution even after all vestige of similarity in primary structure has vanished.