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J. Biol. Chem., Vol. 276, Issue 2, 1304-1310, January 12, 2001

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NMR Analysis of Type III Antifreeze Protein Intramolecular Dimer
STRUCTURAL BASIS FOR ENHANCED ACTIVITY^*

Kazunori Miura, Satoru Ohgiya, Tamotsu Hoshino, Nobuaki Nemoto^§, Tetsuya Suetake, Ai Miura, Leo Spyracopoulos^¶, Hidemasa Kondo, and Sakae Tsuda

 Bioscience and Chemistry Division, Hokkaido National Industrial Research Institute, 2-17-2-1 Tsukisamu-Higashi, Toyohira, Sapporo 062-8517, Japan, ^§ Varian Japan, Varian Japan Sumitomo Shibaura Building, 4-16-36 Shibaura, Minato-ku, Tokyo 108-0023, Japan, and ^¶ Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada

The structure of a new antifreeze protein (AFP) variant, RD3, from antarctic eel pout (Rhigophila dearborni) with enhanced activity has been determined for the first time by nuclear magnetic resonance spectroscopy. RD3 comprises a unique translational topology of two homologous type III AFP globular domains, each containing one flat, ice binding plane. The ice binding plane of the N domain is located ~3.5 Å "behind" that of the C domain. The two ice binding planes are located laterally with an angle of 32 ± 12° between the planes. These results suggest that the C domain plane of RD3 binds first to the ice {100} prism plane in the 0001 direction, which induces successive ice binding of the N domain in the 0101 direction. This manner of ice binding caused by the unique structural topology of RD3 is thought to be crucial for the significant enhancement of antifreeze activity, especially at low AFP concentrations.

The atomic coordinates and the structure factors (code 1C8A and 1C89) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

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