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Science 19 February 1993:
Vol. 259. no. 5098, pp. 1154 - 1157
DOI: 10.1126/science.8438165
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Articles

Science, Vol 259, Issue 5098, 1154-1157
Copyright © 1993 by American Association for the Advancement of Science

articles

The nonhelical structure of antifreeze protein type III

FD Sonnichsen, BD Sykes, H Chao, and PL Davies

Protein Engineering Network of Centres of Excellence, University of Alberta, Edmonton, Canada.

Antifreeze proteins (AFPs) are present in the blood of some marine fishes and inhibit the growth of ice crystals at subzero temperatures by adsorption to the ice lattice. The solution structure of a Type III AFP was determined by two-dimensional nuclear magnetic resonance spectroscopy. These measurements indicate that this 66-residue protein has an unusual fold in which eight beta strands form two sheets of three antiparallel strands and one sheet of two antiparallel strands, and the triple-stranded sheets are packed orthogonally into a beta sandwich. This structure is completely different from the amphipathic, helical structure observed for Type I AFPs.


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