1wfa | pdb_00001wfa
WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT 4 DEGREES C
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Overview
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 A, 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 pair-wise 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 <0112> axes of the (2021) ice planes.
About this Structure
1WFA is a Single protein structure of sequence from Pseudopleuronectes americanus with NH2 as ligand. Full crystallographic information is available from OCA.
Reference
Ice-binding structure and mechanism of an antifreeze protein from winter flounder., Sicheri F, Yang DS, Nature. 1995 Jun 1;375(6530):427-31. PMID:7760940
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