Anchored Clathrate Waters Bind Antifreeze Proteins to Ice
The mechanism by which antifreeze proteins (AFPs) irreversibly bind to ice has not yet been resolved. The ice-binding site of an AFP is relatively hydrophobic, but also contains many potential hydrogen bond donors/acceptors. The extent to which hydrogen bonding and the hydrophobic effect contribute to ice binding has been debated for over 30 years. Here we have elucidated the ice-binding mechanism through solving the first crystal structure of an Antarctic bacterial AFP. This 34-kDa domain, the largest AFP structure determined to date, folds as a Ca{sup 2+}-bound parallel beta-helix with an extensive array of ice-like surface waters that are anchored via hydrogen bonds directly to the polypeptide backbone and adjacent side chains. These bound waters make an excellent three-dimensional match to both the primary prism and basal planes of ice and in effect provide an extensive X-ray crystallographic picture of the AFP{vert_ellipsis}ice interaction. This unobstructed view, free from crystal-packing artefacts, shows the contributions of both the hydrophobic effect and hydrogen bonding during AFP adsorption to ice. We term this mode of binding the 'anchored clathrate' mechanism of AFP action.
- Research Organization:
- Brookhaven National Lab. (BNL), Upton, NY (United States)
- Sponsoring Organization:
- USDOE SC OFFICE OF SCIENCE (SC)
- DOE Contract Number:
- DE-AC02-98CH10886
- OSTI ID:
- 1041660
- Report Number(s):
- BNL-97338-2012-JA; PNASA6; TRN: US201212%%78
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America, Vol. 108, Issue 18; ISSN 0027-8424
- Country of Publication:
- United States
- Language:
- English
Similar Records
An Antifreeze Protein Folds with an Interior Network of More Than 400 Semi-Clathrate Waters
Structure and Evolutionary Origin of Ca2+-Dependent Herring Type II Antifreeze Protein