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Related Experiment Videos

Identification of the ice-binding surface on a type III antifreeze protein with a "flatness function" algorithm

D S Yang1, W C Hon, S Bubanko

  • 1Department of Biochemistry, Faculty of Health Science, McMaster University, Hamilton, Ontario, Canada. yang@xtliris.csu.mcmaster.ca

Biophysical Journal
|May 20, 1998
PubMed
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Antifreeze proteins (AFPs) bind to ice crystals to stop growth. This study shows ice-binding surface (IBS) identification in type III AFPs relies on surface flatness, not just polar interactions.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Cryobiology

Background:

  • Antifreeze proteins (AFPs) prevent ice crystal growth by adsorbing to ice surfaces.
  • Current hypotheses focus on hydrophilic interactions and hydrogen bonding for AFP binding affinity and specificity.
  • Type III AFPs, unlike other types, have a globular structure, making their ice-binding surface (IBS) less obvious.

Purpose of the Study:

  • To determine the crystal structure of a type III AFP (HPLC-3) from ocean pout.
  • To identify the ice-binding surface (IBS) of this globular type III AFP.
  • To test the hypothesis that surface flatness is a key factor in identifying the IBS.

Main Methods:

  • X-ray crystallography was used to determine the 2.0-A resolution structure of HPLC-3.

Related Experiment Videos

  • An automated algorithm was developed to analyze surface planarity and identify potential IBS.
  • The identified IBS was compared with results from previous mutagenesis studies.

    • Main Results:

    • The crystal structure revealed an internal dyad motif in the type III AFP.
    • The automated algorithm identified a specific loop as the IBS, matching previous mutagenesis findings.
    • The identified IBS has a high degree of surface flatness and significant nonpolar surface area (67%).

    Conclusions:

    • Surface flatness is a primary factor for identifying the ice-binding surface (IBS) of antifreeze proteins (AFPs), even for globular type III AFPs.
    • The IBS identification algorithm successfully located the functional surface without relying on polar interactions.
    • Surface complementarity is proposed as the mechanism for AFP specificity with different ice crystal planes.