STRUCTURAL SIMILARITY OF DNA-BINDING DOMAINS OF BACTERIOPHAGE REPRESSORS AND THE GLOBIN CORE

Background: In recent years, the determination of large numbers of protein structures has created a need for automatic and objective methods for the comparison of structures or conformations. Many protein structures show similarities of conformation that are undetectable by comparing their sequences. Comparison of structures can reveal similarities between proteins thought to be unrelated, providing new insight into the interrelationships of sequence, structure and function. Results: Using a new tool that we have developed to perform rapid structural alignment, we present the highlights of an exhaustive comparison of all pairs of protein structures in the Brookhaven protein database. Notably, we find that the DNA-binding domain of the bacteriophage repressor family is almost completely embedded in the larger eight-helix fold of the globin family of proteins. The significant match of specific residues is correlated with functional, structural and evolutionary in formation. Conclusion: Our method can help to identify structurally similar folds rapidly and with high-sensitivity, providing a powerful tool for analyzing the ever-increasing number of protein structures being elucidated.