Characterization of microbial antifreeze protein with intermediate activity suggests that a bound-water network is essential for hyperactivity

Abstract Antifreeze proteins (AFPs) inhibit ice growth by adsorbing onto specific ice planes. Microbial AFPs show diverse antifreeze activity and ice plane specificity, while sharing a common molecular scaffold. To probe the molecular mechanisms responsible for AFP activity, we here characterized th...

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Autores principales:	N. M.-Mofiz Uddin Khan, Tatsuya Arai, Sakae Tsuda, Hidemasa Kondo
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/42ba24df757847b982ec72a948e08652
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spelling	oai:doaj.org-article:42ba24df757847b982ec72a948e086522021-12-02T13:17:49ZCharacterization of microbial antifreeze protein with intermediate activity suggests that a bound-water network is essential for hyperactivity10.1038/s41598-021-85559-x2045-2322https://doaj.org/article/42ba24df757847b982ec72a948e086522021-03-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-85559-xhttps://doaj.org/toc/2045-2322Abstract Antifreeze proteins (AFPs) inhibit ice growth by adsorbing onto specific ice planes. Microbial AFPs show diverse antifreeze activity and ice plane specificity, while sharing a common molecular scaffold. To probe the molecular mechanisms responsible for AFP activity, we here characterized the antifreeze activity and crystal structure of TisAFP7 from the snow mold fungus Typhula ishikariensis. TisAFP7 exhibited intermediate activity, with the ability to bind the basal plane, compared with a hyperactive isoform TisAFP8 and a moderately active isoform TisAFP6. Analysis of the TisAFP7 crystal structure revealed a bound-water network arranged in a zigzag pattern on the surface of the protein’s ice-binding site (IBS). While the three AFP isoforms shared the water network pattern, the network on TisAFP7 IBS was not extensive, which was likely related to its intermediate activity. Analysis of the TisAFP7 crystal structure also revealed the presence of additional water molecules that form a ring-like network surrounding the hydrophobic side chain of a crucial IBS phenylalanine, which might be responsible for the increased adsorption of AFP molecule onto the basal plane. Based on these observations, we propose that the extended water network and hydrophobic hydration at IBS together determine the TisAFP activity.N. M.-Mofiz Uddin KhanTatsuya AraiSakae TsudaHidemasa KondoNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-15 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q N. M.-Mofiz Uddin Khan Tatsuya Arai Sakae Tsuda Hidemasa Kondo Characterization of microbial antifreeze protein with intermediate activity suggests that a bound-water network is essential for hyperactivity
description	Abstract Antifreeze proteins (AFPs) inhibit ice growth by adsorbing onto specific ice planes. Microbial AFPs show diverse antifreeze activity and ice plane specificity, while sharing a common molecular scaffold. To probe the molecular mechanisms responsible for AFP activity, we here characterized the antifreeze activity and crystal structure of TisAFP7 from the snow mold fungus Typhula ishikariensis. TisAFP7 exhibited intermediate activity, with the ability to bind the basal plane, compared with a hyperactive isoform TisAFP8 and a moderately active isoform TisAFP6. Analysis of the TisAFP7 crystal structure revealed a bound-water network arranged in a zigzag pattern on the surface of the protein’s ice-binding site (IBS). While the three AFP isoforms shared the water network pattern, the network on TisAFP7 IBS was not extensive, which was likely related to its intermediate activity. Analysis of the TisAFP7 crystal structure also revealed the presence of additional water molecules that form a ring-like network surrounding the hydrophobic side chain of a crucial IBS phenylalanine, which might be responsible for the increased adsorption of AFP molecule onto the basal plane. Based on these observations, we propose that the extended water network and hydrophobic hydration at IBS together determine the TisAFP activity.
format	article
author	N. M.-Mofiz Uddin Khan Tatsuya Arai Sakae Tsuda Hidemasa Kondo
author_facet	N. M.-Mofiz Uddin Khan Tatsuya Arai Sakae Tsuda Hidemasa Kondo
author_sort	N. M.-Mofiz Uddin Khan
title	Characterization of microbial antifreeze protein with intermediate activity suggests that a bound-water network is essential for hyperactivity
title_short	Characterization of microbial antifreeze protein with intermediate activity suggests that a bound-water network is essential for hyperactivity
title_full	Characterization of microbial antifreeze protein with intermediate activity suggests that a bound-water network is essential for hyperactivity
title_fullStr	Characterization of microbial antifreeze protein with intermediate activity suggests that a bound-water network is essential for hyperactivity
title_full_unstemmed	Characterization of microbial antifreeze protein with intermediate activity suggests that a bound-water network is essential for hyperactivity
title_sort	characterization of microbial antifreeze protein with intermediate activity suggests that a bound-water network is essential for hyperactivity
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/42ba24df757847b982ec72a948e08652
work_keys_str_mv	AT nmmofizuddinkhan characterizationofmicrobialantifreezeproteinwithintermediateactivitysuggeststhataboundwaternetworkisessentialforhyperactivity AT tatsuyaarai characterizationofmicrobialantifreezeproteinwithintermediateactivitysuggeststhataboundwaternetworkisessentialforhyperactivity AT sakaetsuda characterizationofmicrobialantifreezeproteinwithintermediateactivitysuggeststhataboundwaternetworkisessentialforhyperactivity AT hidemasakondo characterizationofmicrobialantifreezeproteinwithintermediateactivitysuggeststhataboundwaternetworkisessentialforhyperactivity
_version_	1718393327960719360

Characterization of microbial antifreeze protein with intermediate activity suggests that a bound-water network is essential for hyperactivity

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