Hydrogen-deuterium exchange mass spectrometry captures distinct dynamics upon substrate and inhibitor binding to a transporter

XylE is a bacterial xylose transporter and homologue of human glucose transporters GLUTs 1-4. HDX-MS, mutagenesis and MD simulations suggest that protonation of a conserved aspartate triggers conformational transition from outward- to inward facing state only in the presence of substrate xylose. In...

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Autores principales:	Ruyu Jia, Chloe Martens, Mrinal Shekhar, Shashank Pant, Grant A. Pellowe, Andy M. Lau, Heather E. Findlay, Nicola J. Harris, Emad Tajkhorshid, Paula J. Booth, Argyris Politis
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/d6cb78ca4eb8432388486c3f0d334672
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spelling	oai:doaj.org-article:d6cb78ca4eb8432388486c3f0d3346722021-12-02T17:32:59ZHydrogen-deuterium exchange mass spectrometry captures distinct dynamics upon substrate and inhibitor binding to a transporter10.1038/s41467-020-20032-32041-1723https://doaj.org/article/d6cb78ca4eb8432388486c3f0d3346722020-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20032-3https://doaj.org/toc/2041-1723XylE is a bacterial xylose transporter and homologue of human glucose transporters GLUTs 1-4. HDX-MS, mutagenesis and MD simulations suggest that protonation of a conserved aspartate triggers conformational transition from outward- to inward facing state only in the presence of substrate xylose. In contrast, inhibitor glucose locks the transporter in the outward facing state.Ruyu JiaChloe MartensMrinal ShekharShashank PantGrant A. PelloweAndy M. LauHeather E. FindlayNicola J. HarrisEmad TajkhorshidPaula J. BoothArgyris PolitisNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Ruyu Jia Chloe Martens Mrinal Shekhar Shashank Pant Grant A. Pellowe Andy M. Lau Heather E. Findlay Nicola J. Harris Emad Tajkhorshid Paula J. Booth Argyris Politis Hydrogen-deuterium exchange mass spectrometry captures distinct dynamics upon substrate and inhibitor binding to a transporter
description	XylE is a bacterial xylose transporter and homologue of human glucose transporters GLUTs 1-4. HDX-MS, mutagenesis and MD simulations suggest that protonation of a conserved aspartate triggers conformational transition from outward- to inward facing state only in the presence of substrate xylose. In contrast, inhibitor glucose locks the transporter in the outward facing state.
format	article
author	Ruyu Jia Chloe Martens Mrinal Shekhar Shashank Pant Grant A. Pellowe Andy M. Lau Heather E. Findlay Nicola J. Harris Emad Tajkhorshid Paula J. Booth Argyris Politis
author_facet	Ruyu Jia Chloe Martens Mrinal Shekhar Shashank Pant Grant A. Pellowe Andy M. Lau Heather E. Findlay Nicola J. Harris Emad Tajkhorshid Paula J. Booth Argyris Politis
author_sort	Ruyu Jia
title	Hydrogen-deuterium exchange mass spectrometry captures distinct dynamics upon substrate and inhibitor binding to a transporter
title_short	Hydrogen-deuterium exchange mass spectrometry captures distinct dynamics upon substrate and inhibitor binding to a transporter
title_full	Hydrogen-deuterium exchange mass spectrometry captures distinct dynamics upon substrate and inhibitor binding to a transporter
title_fullStr	Hydrogen-deuterium exchange mass spectrometry captures distinct dynamics upon substrate and inhibitor binding to a transporter
title_full_unstemmed	Hydrogen-deuterium exchange mass spectrometry captures distinct dynamics upon substrate and inhibitor binding to a transporter
title_sort	hydrogen-deuterium exchange mass spectrometry captures distinct dynamics upon substrate and inhibitor binding to a transporter
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/d6cb78ca4eb8432388486c3f0d334672
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Hydrogen-deuterium exchange mass spectrometry captures distinct dynamics upon substrate and inhibitor binding to a transporter

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