Abstract
The X-ray crystallographic structure of an antifreeze polypeptide from the fish winter flounder, has been determined at 2.5 Å by an analysis of the Patter son function. This is the first report of a polypeptide of this size that is a single α-helix. A proposed mechanism of antifreeze binding to ice surfaces is given which requires: first, that the dipole moment from the helical structure dictates the preferential alignment of the peptide to the c-axis of ice nuclei; second, amphiphilicity of the helix; and third, torsional freedom of the side chains to facilitate hydrogen bonding to ice surfaces.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
DeVries, A. L. Phil. Trans. R. Soc. B304, 575–588 (1984).
Hew, C. L. & Fletcher, G. L. in Circulation, Respiration and Metabolism (ed. Gilles, R.) 553–563 (Springer, Berlin, 1985).
Feeney, R. E., Burcham, T. S. & Yeh, Y. Ann. Rev. Biophys. biophys. Chem. 15, 59–78 (1986).
Hew, C. L., Scott, G. K. & Davis, P. L. in Living in the Cold, Physiological and Biochemical Adaptation (eds Heller, H. D. et al.) 117–123 (Elsevier, New York, 1986).
Berman, E., Allerhand, A. & DeVries, A. L. J. biol. Chem. 255, 4407–4410 (1980).
Hol, W. G. J., van Duijnen, P. T. & Berendsen, H. J. C. Nature 273, 443–446 (1978).
Shoemaker, K. R. et al. Nature 326, 563–567 (1987).
Davies, P. L., Roach, A. H. & Hew, C. L. Proc. natn. Acad. Sci. U.S.A. 79, 335–339 (1982).
Pickett, M. H. et al. Eur. J. Biochem. 143, 35–38 (1985).
Chakrabartty, A. et al. Can. J. Zool. (in the press).
Ananthanarayanan, V. S. & Hew, C. L. Biochem. biophys. Res. Commun. 74, 685–689 (1977).
Yang, D. S. C., Chung, Y. J., Chen, P., Rose, J. P. & Hew, C. L. J. molec. Biol. 189, 725–725 (1986).
Patterson, A. L. Z. Kristallogr. 90, 517–521 (1935).
Yang, D. S. C. thesis, Univ. Pittsburgh (1983).
Furey, W. et al. J. appl. Crystallogr. 15, 160–166 (1982).
Hendrickson, W. A. & Konnert, J. H. Biomolec. Struct. Funct. Conform. Evol. Vol. I, 43–57 (1981).
Svensson, L. A. et al. Proteins: Struct. Funct. Genet. 1, 370–375 (1986).
Fletcher, N. H. The Chemical Physics of Ice (Cambridge University Press, 1970).
Raymond, J. A. & DeVries, A. L. Proc. natn. Acad. Sci. U.S.A. 74, 2589–2593 (1977).
DeVries, A. L. & Lin, Y. Biochim. biophys. Acta 495, 388–392 (1977).
Knight, C. A., DeVries, A. L. & Oolman, L. D. Nature 308, 295–296 (1984).
Eisenberg, D., Weiss, D. & Terwilliger, T. C. Nature 299, 371–374 (1982).
Eisenberg, D., Schwarz, E., Komaromy, M. & Wall, E. J. molec. Biol. 179, 125–142 (1984).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Yang, D., Sax, M., Chakrabartty, A. et al. Crystal structure of an antifreeze polypeptide and its mechanistic implications. Nature 333, 232–237 (1988). https://doi.org/10.1038/333232a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/333232a0
- Springer Nature Limited
This article is cited by
-
Structural diversity of marine anti-freezing proteins, properties and potential applications: a review
Bioresources and Bioprocessing (2022)
-
Mechanisms of antifreeze proteins investigated via the site-directed spin labeling technique
European Biophysics Journal (2018)
-
Concentration-dependent oligomerization of an alpha-helical antifreeze polypeptide makes it hyperactive
Scientific Reports (2017)
-
Role of ice structuring proteins on freezing–thawing cycles of pasta sauces
Journal of Food Science and Technology (2016)
-
Effects of a type I antifreeze protein (AFP) on the melting of frozen AFP and AFP+solute aqueous solutions studied by NMR microimaging experiment
Journal of Biological Physics (2013)