ICE-BINDING STRUCTURE AND MECHANISM OF AN ANTIFREEZE PROTEIN FROM WINTER FLOUNDER

ANTIFREEZE proteins provide fish with protection against the freezing effect of polar environments by binding to ice surfaces and inhibiting growth of ice crystals. We present the X-ray crystal structure at 1.5 Angstrom resolution of a lone alpha-helical antifreeze protein from winter flounder, which provides a detailed look at its ice-binding features. These consist of four repeated ice-binding motifs, the side chains of which are inherently rigid or restrained by pairwise side-chain interactions to form a flat binding surface. Elaborate amino- and carboxy-terminal cap structures are also present, which explain the protein's rich alpha-helical content in solution. We propose an ice-binding model that accounts for the binding specificity of the antifreeze protein along the [01 (1) over bar 2] axes of the {20 (2) over bar 1} ice planes(1).