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Mimicry of ice structure by surface hydroxyls and water of a β-helix antifreeze protein

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  • Yih-Cherng Liou

    (Queen's University)

  • Ante Tocilj

    (Queen's University)

  • Peter L. Davies

    (Queen's University)

  • Zongchao Jia

    (Queen's University)

Abstract

Insect antifreeze proteins (AFP) are much more effective than fish AFPs at depressing solution freezing points by ice-growth inhibition1,2. AFP from the beetle Tenebrio molitor is a small protein (8.4 kDa) composed of tandem 12-residue repeats3 (TCTxSxxCxxAx). Here we report its 1.4-Å resolution crystal structure, showing that this repetitive sequence translates into an exceptionally regular β-helix. Not only are the 12-amino-acid loops almost identical in the backbone, but also the conserved side chains are positioned in essentially identical orientations, making this AFP perhaps the most regular protein structure yet observed. The protein has almost no hydrophobic core but is stabilized by numerous disulphide and hydrogen bonds. On the conserved side of the protein, threonine-cysteine-threonine motifs are arrayed to form a flat β-sheet, the putative ice-binding surface. The threonine side chains have exactly the same rotameric conformation and the spacing between OH groups is a near-perfect match to the ice lattice. Together with tightly bound co-planar external water, three ranks of oxygen atoms form a two-dimensional array, mimicking an ice section.

Suggested Citation

  • Yih-Cherng Liou & Ante Tocilj & Peter L. Davies & Zongchao Jia, 2000. "Mimicry of ice structure by surface hydroxyls and water of a β-helix antifreeze protein," Nature, Nature, vol. 406(6793), pages 322-324, July.
    • Handle: RePEc:nat:nature:v:406:y:2000:i:6793:d:10.1038_35018604
    DOI: 10.1038/35018604
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    Cited by:

    1. Alireza Hakimian & Mohammadjavad Mohebinia & Masoumeh Nazari & Ali Davoodabadi & Sina Nazifi & Zixu Huang & Jiming Bao & Hadi Ghasemi, 2021. "Freezing of few nanometers water droplets," Nature Communications, Nature, vol. 12(1), pages 1-8, December.
    2. Jordan Forbes & Akalabya Bissoyi & Lukas Eickhoff & Naama Reicher & Thomas Hansen & Christopher G. Bon & Virginia K. Walker & Thomas Koop & Yinon Rudich & Ido Braslavsky & Peter L. Davies, 2022. "Water-organizing motif continuity is critical for potent ice nucleation protein activity," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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