Elucidation of protein architecture and molecular evolution of microbial antifreeze proteins

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Antifreeze proteins bind preferentially to the surfaces of embryonic ice crystals and inhibit further growth of ice. In the present study we analyzed three-dimensional structures of microbial antifreeze proteins and revealed their possible ice-binding site by structure-based site-directed mutagenesis. Antifreeze activities measured for various kinds of microbial antifreeze proteins exhibited wide diversity both in thermal hysteresis value and ice crystal shape, in spite of their high sequence homologies. From these observations it is suggested that microbial antifreeze proteins share a common structural scaffold for their interaction with ice and adopt their own antifreeze activities according to their growing environment.