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...
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ftpubmed:oai:pubmedcentral.nih.gov:3088597 2023-05-15T13:54:36+02:00 Anchored clathrate waters bind antifreeze proteins to ice Garnham, Christopher P. Campbell, Robert L. Davies, Peter L. 2011-05-03 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3088597 http://www.ncbi.nlm.nih.gov/pubmed/21482800 https://doi.org/10.1073/pnas.1100429108 en eng National Academy of Sciences http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3088597 http://www.ncbi.nlm.nih.gov/pubmed/21482800 http://dx.doi.org/10.1073/pnas.1100429108 Freely available online through the PNAS open access option. Biological Sciences Text 2011 ftpubmed https://doi.org/10.1073/pnas.1100429108 2013-09-03T14:14:12Z 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 Ca2+-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∶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. Text Antarc* Antarctic PubMed Central (PMC) Antarctic Proceedings of the National Academy of Sciences 108 18 7363 7367 |
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Biological Sciences |
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Biological Sciences Garnham, Christopher P. Campbell, Robert L. Davies, Peter L. Anchored clathrate waters bind antifreeze proteins to ice |
topic_facet |
Biological Sciences |
description |
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 Ca2+-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∶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. |
format |
Text |
author |
Garnham, Christopher P. Campbell, Robert L. Davies, Peter L. |
author_facet |
Garnham, Christopher P. Campbell, Robert L. Davies, Peter L. |
author_sort |
Garnham, Christopher P. |
title |
Anchored clathrate waters bind antifreeze proteins to ice |
title_short |
Anchored clathrate waters bind antifreeze proteins to ice |
title_full |
Anchored clathrate waters bind antifreeze proteins to ice |
title_fullStr |
Anchored clathrate waters bind antifreeze proteins to ice |
title_full_unstemmed |
Anchored clathrate waters bind antifreeze proteins to ice |
title_sort |
anchored clathrate waters bind antifreeze proteins to ice |
publisher |
National Academy of Sciences |
publishDate |
2011 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3088597 http://www.ncbi.nlm.nih.gov/pubmed/21482800 https://doi.org/10.1073/pnas.1100429108 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3088597 http://www.ncbi.nlm.nih.gov/pubmed/21482800 http://dx.doi.org/10.1073/pnas.1100429108 |
op_rights |
Freely available online through the PNAS open access option. |
op_doi |
https://doi.org/10.1073/pnas.1100429108 |
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Proceedings of the National Academy of Sciences |
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108 |
container_issue |
18 |
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7363 |
op_container_end_page |
7367 |
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1766260582899515392 |