An Ice-Binding Protein from an Antarctic Ascomycete Is Fine-Tuned to Bind to Specific Water Molecules Located in the Ice Prism Planes
Many microbes that survive in cold environments are known to secrete ice-binding proteins (IBPs). The structure–function relationship of these proteins remains unclear. A microbial IBP denoted Anp IBP was recently isolated from a cold-adapted fungus, Antarctomyces psychrotrophicus . The present stud...
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ftdoajarticles:oai:doaj.org/article:26e9c8058b1d447c94f56c5eab55d98a 2023-05-15T14:01:45+02:00 An Ice-Binding Protein from an Antarctic Ascomycete Is Fine-Tuned to Bind to Specific Water Molecules Located in the Ice Prism Planes Akari Yamauchi Tatsuya Arai Hidemasa Kondo Yuji C. Sasaki Sakae Tsuda 2020-05-01T00:00:00Z https://doi.org/10.3390/biom10050759 https://doaj.org/article/26e9c8058b1d447c94f56c5eab55d98a EN eng MDPI AG https://www.mdpi.com/2218-273X/10/5/759 https://doaj.org/toc/2218-273X doi:10.3390/biom10050759 2218-273X https://doaj.org/article/26e9c8058b1d447c94f56c5eab55d98a Biomolecules, Vol 10, Iss 759, p 759 (2020) ice-binding protein antifreeze protein ascomycete thermal hysteresis fluorescence-based ice plane affinity polygonal waters Microbiology QR1-502 article 2020 ftdoajarticles https://doi.org/10.3390/biom10050759 2022-12-31T12:43:24Z Many microbes that survive in cold environments are known to secrete ice-binding proteins (IBPs). The structure–function relationship of these proteins remains unclear. A microbial IBP denoted Anp IBP was recently isolated from a cold-adapted fungus, Antarctomyces psychrotrophicus . The present study identified an orbital illumination (prism ring) on a globular single ice crystal when soaked in a solution of fluorescent Anp IBP, suggesting that Anp IBP binds to specific water molecules located in the ice prism planes. In order to examine this unique ice-binding mechanism, we carried out X-ray structural analysis and mutational experiments. It appeared that Anp IBP is made of 6-ladder β-helices with a triangular cross section that accompanies an “ice-like” water network on the ice-binding site. The network, however, does not exist in a defective mutant. Anp IBP has a row of four unique hollows on the IBS, where the distance between the hollows (14.7 Å) is complementary to the oxygen atom spacing of the prism ring. These results suggest the structure of Anp IBP is fine-tuned to merge with the ice–water interface of an ice crystal through its polygonal water network and is then bound to a specific set of water molecules constructing the prism ring to effectively halt the growth of ice. Article in Journal/Newspaper Antarc* Antarctic Directory of Open Access Journals: DOAJ Articles Antarctic Biomolecules 10 5 759 |
institution |
Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
ice-binding protein antifreeze protein ascomycete thermal hysteresis fluorescence-based ice plane affinity polygonal waters Microbiology QR1-502 |
spellingShingle |
ice-binding protein antifreeze protein ascomycete thermal hysteresis fluorescence-based ice plane affinity polygonal waters Microbiology QR1-502 Akari Yamauchi Tatsuya Arai Hidemasa Kondo Yuji C. Sasaki Sakae Tsuda An Ice-Binding Protein from an Antarctic Ascomycete Is Fine-Tuned to Bind to Specific Water Molecules Located in the Ice Prism Planes |
topic_facet |
ice-binding protein antifreeze protein ascomycete thermal hysteresis fluorescence-based ice plane affinity polygonal waters Microbiology QR1-502 |
description |
Many microbes that survive in cold environments are known to secrete ice-binding proteins (IBPs). The structure–function relationship of these proteins remains unclear. A microbial IBP denoted Anp IBP was recently isolated from a cold-adapted fungus, Antarctomyces psychrotrophicus . The present study identified an orbital illumination (prism ring) on a globular single ice crystal when soaked in a solution of fluorescent Anp IBP, suggesting that Anp IBP binds to specific water molecules located in the ice prism planes. In order to examine this unique ice-binding mechanism, we carried out X-ray structural analysis and mutational experiments. It appeared that Anp IBP is made of 6-ladder β-helices with a triangular cross section that accompanies an “ice-like” water network on the ice-binding site. The network, however, does not exist in a defective mutant. Anp IBP has a row of four unique hollows on the IBS, where the distance between the hollows (14.7 Å) is complementary to the oxygen atom spacing of the prism ring. These results suggest the structure of Anp IBP is fine-tuned to merge with the ice–water interface of an ice crystal through its polygonal water network and is then bound to a specific set of water molecules constructing the prism ring to effectively halt the growth of ice. |
format |
Article in Journal/Newspaper |
author |
Akari Yamauchi Tatsuya Arai Hidemasa Kondo Yuji C. Sasaki Sakae Tsuda |
author_facet |
Akari Yamauchi Tatsuya Arai Hidemasa Kondo Yuji C. Sasaki Sakae Tsuda |
author_sort |
Akari Yamauchi |
title |
An Ice-Binding Protein from an Antarctic Ascomycete Is Fine-Tuned to Bind to Specific Water Molecules Located in the Ice Prism Planes |
title_short |
An Ice-Binding Protein from an Antarctic Ascomycete Is Fine-Tuned to Bind to Specific Water Molecules Located in the Ice Prism Planes |
title_full |
An Ice-Binding Protein from an Antarctic Ascomycete Is Fine-Tuned to Bind to Specific Water Molecules Located in the Ice Prism Planes |
title_fullStr |
An Ice-Binding Protein from an Antarctic Ascomycete Is Fine-Tuned to Bind to Specific Water Molecules Located in the Ice Prism Planes |
title_full_unstemmed |
An Ice-Binding Protein from an Antarctic Ascomycete Is Fine-Tuned to Bind to Specific Water Molecules Located in the Ice Prism Planes |
title_sort |
ice-binding protein from an antarctic ascomycete is fine-tuned to bind to specific water molecules located in the ice prism planes |
publisher |
MDPI AG |
publishDate |
2020 |
url |
https://doi.org/10.3390/biom10050759 https://doaj.org/article/26e9c8058b1d447c94f56c5eab55d98a |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Biomolecules, Vol 10, Iss 759, p 759 (2020) |
op_relation |
https://www.mdpi.com/2218-273X/10/5/759 https://doaj.org/toc/2218-273X doi:10.3390/biom10050759 2218-273X https://doaj.org/article/26e9c8058b1d447c94f56c5eab55d98a |
op_doi |
https://doi.org/10.3390/biom10050759 |
container_title |
Biomolecules |
container_volume |
10 |
container_issue |
5 |
container_start_page |
759 |
_version_ |
1766271790056734720 |