Temperature dependence of protein-water interactions in a gated yeast aquaporin

Abstract Regulation of aquaporins is a key process of living organisms to counteract sudden osmotic changes. Aqy1, which is a water transporting aquaporin of the yeast Pichia pastoris, is suggested to be gated by chemo-mechanical stimuli as a protective regulatory-response against rapid freezing. He...

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Autores principales:	Camilo Aponte-Santamaría, Gerhard Fischer, Petra Båth, Richard Neutze, Bert L. de Groot
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f8bf4274f74b4368bf0c7690b708c42d
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spelling	oai:doaj.org-article:f8bf4274f74b4368bf0c7690b708c42d2021-12-02T12:30:13ZTemperature dependence of protein-water interactions in a gated yeast aquaporin10.1038/s41598-017-04180-z2045-2322https://doaj.org/article/f8bf4274f74b4368bf0c7690b708c42d2017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-04180-zhttps://doaj.org/toc/2045-2322Abstract Regulation of aquaporins is a key process of living organisms to counteract sudden osmotic changes. Aqy1, which is a water transporting aquaporin of the yeast Pichia pastoris, is suggested to be gated by chemo-mechanical stimuli as a protective regulatory-response against rapid freezing. Here, we tested the influence of temperature by determining the X-ray structure of Aqy1 at room temperature (RT) at 1.3 Å resolution, and by exploring the structural dynamics of Aqy1 during freezing through molecular dynamics simulations. At ambient temperature and in a lipid bilayer, Aqy1 adopts a closed conformation that is globally better described by the RT than by the low-temperature (LT) crystal structure. Locally, for the blocking-residue Tyr31 and the water molecules inside the pore, both LT and RT data sets are consistent with the positions observed in the simulations at room-temperature. Moreover, as the temperature was lowered, Tyr31 adopted a conformation that more effectively blocked the channel, and its motion was accompanied by a temperature-driven rearrangement of the water molecules inside the channel. We therefore speculate that temperature drives Aqy1 from a loosely- to a tightly-blocked state. This analysis provides high-resolution structural evidence of the influence of temperature on membrane-transport channels.Camilo Aponte-SantamaríaGerhard FischerPetra BåthRichard NeutzeBert L. de GrootNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Camilo Aponte-Santamaría Gerhard Fischer Petra Båth Richard Neutze Bert L. de Groot Temperature dependence of protein-water interactions in a gated yeast aquaporin
description	Abstract Regulation of aquaporins is a key process of living organisms to counteract sudden osmotic changes. Aqy1, which is a water transporting aquaporin of the yeast Pichia pastoris, is suggested to be gated by chemo-mechanical stimuli as a protective regulatory-response against rapid freezing. Here, we tested the influence of temperature by determining the X-ray structure of Aqy1 at room temperature (RT) at 1.3 Å resolution, and by exploring the structural dynamics of Aqy1 during freezing through molecular dynamics simulations. At ambient temperature and in a lipid bilayer, Aqy1 adopts a closed conformation that is globally better described by the RT than by the low-temperature (LT) crystal structure. Locally, for the blocking-residue Tyr31 and the water molecules inside the pore, both LT and RT data sets are consistent with the positions observed in the simulations at room-temperature. Moreover, as the temperature was lowered, Tyr31 adopted a conformation that more effectively blocked the channel, and its motion was accompanied by a temperature-driven rearrangement of the water molecules inside the channel. We therefore speculate that temperature drives Aqy1 from a loosely- to a tightly-blocked state. This analysis provides high-resolution structural evidence of the influence of temperature on membrane-transport channels.
format	article
author	Camilo Aponte-Santamaría Gerhard Fischer Petra Båth Richard Neutze Bert L. de Groot
author_facet	Camilo Aponte-Santamaría Gerhard Fischer Petra Båth Richard Neutze Bert L. de Groot
author_sort	Camilo Aponte-Santamaría
title	Temperature dependence of protein-water interactions in a gated yeast aquaporin
title_short	Temperature dependence of protein-water interactions in a gated yeast aquaporin
title_full	Temperature dependence of protein-water interactions in a gated yeast aquaporin
title_fullStr	Temperature dependence of protein-water interactions in a gated yeast aquaporin
title_full_unstemmed	Temperature dependence of protein-water interactions in a gated yeast aquaporin
title_sort	temperature dependence of protein-water interactions in a gated yeast aquaporin
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/f8bf4274f74b4368bf0c7690b708c42d
work_keys_str_mv	AT camiloapontesantamaria temperaturedependenceofproteinwaterinteractionsinagatedyeastaquaporin AT gerhardfischer temperaturedependenceofproteinwaterinteractionsinagatedyeastaquaporin AT petrabath temperaturedependenceofproteinwaterinteractionsinagatedyeastaquaporin AT richardneutze temperaturedependenceofproteinwaterinteractionsinagatedyeastaquaporin AT bertldegroot temperaturedependenceofproteinwaterinteractionsinagatedyeastaquaporin
_version_	1718394432515997696

Temperature dependence of protein-water interactions in a gated yeast aquaporin

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