Goose lysozyme structure: an evolutionary link between hen and bacteriophage lysozymes?
During evolution, the amino acid sequence of a protein is much more variable and changes more rapidly than its tertiary structure. Given sufficient time, the amino acid sequences of proteins derived from a common precursor may alter to the point that they are no longer demonstrably homologous. The ability to make meaningful comparisons between such distantly related proteins must therefore come primarily from structural homology, and only secondarily (if at all) from sequence homology. On the other hand, structural homology in the absence of sequence homology might be attributed to convergent rather than divergent evolution. (A common fold might be dictated by functional or folding requirements.) We have previously argued, on the basis of structural and functional similarities, that the lysozymes of hen egg-white and bacteriophage T4 have a common evolutionary precursor, even though their amino acid sequences have no detectable similarity. Here we report the structure of the lysozyme from Embden goose, a representative of a third class of lysozymes that has no sequence homology (or perhaps very weak homology) with either the hen egg-white or the phage enzyme. The structure of goose egg-white lysozyme has striking similarities to the lysozymes from hen egg-white and bacteriophage T4. However, some parts of goose lysozyme resemble hen lysozyme while other parts correspond only to the phage enzyme. The nature of the structural correspondence strongly suggests that all three lysozymes evolved from a common precursor.
D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D004527:Egg Proteins; D005777:Geese; D008958:Models, Molecular; D009113:Muramidase; D011487:Protein Conformation; D013604:T-Phages
D004527:Egg Proteins; D009113:Muramidase