Structural Evidence for Evolution of the β/α Barrel Scaffold by Gene Duplication and Fusion

Abstract

The atomic structures of two proteins in the histidine biosynthesis pathway consist of β/α barrels with a twofold repeat pattern. It is likely that these proteins evolved by twofold gene duplication and gene fusion from a common half-barrel ancestor. These ancestral domains are not visible as independent domains in the extant proteins but can be inferred from a combination of sequence and structural analysis. The detection of subdomain structures may be useful in efforts to search genome sequences for functionally and structurally related proteins.