A conserved leucine occupies the empty substrate site of LeuT in the Na+-free return state

Neurotransmitter:sodium symporters (NSS) perform Na+-dependent amino-acid uptake, but a full structural description of their function is lacking. Here the authors present a structure of the bacterial NSS LeuT in the outward-oriented empty state and show that a Leu residue occupies the empty substrat...

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Autores principales:	Lina Malinauskaite, Saida Said, Caglanur Sahin, Julie Grouleff, Azadeh Shahsavar, Henriette Bjerregaard, Pernille Noer, Kasper Severinsen, Thomas Boesen, Birgit Schiøtt, Steffen Sinning, Poul Nissen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/0c4dfaf71bb84eee82b29dd34e8c741a
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spelling	oai:doaj.org-article:0c4dfaf71bb84eee82b29dd34e8c741a2021-12-02T15:34:51ZA conserved leucine occupies the empty substrate site of LeuT in the Na+-free return state10.1038/ncomms116732041-1723https://doaj.org/article/0c4dfaf71bb84eee82b29dd34e8c741a2016-05-01T00:00:00Zhttps://doi.org/10.1038/ncomms11673https://doaj.org/toc/2041-1723Neurotransmitter:sodium symporters (NSS) perform Na+-dependent amino-acid uptake, but a full structural description of their function is lacking. Here the authors present a structure of the bacterial NSS LeuT in the outward-oriented empty state and show that a Leu residue occupies the empty substrate site and is essential for function.Lina MalinauskaiteSaida SaidCaglanur SahinJulie GrouleffAzadeh ShahsavarHenriette BjerregaardPernille NoerKasper SeverinsenThomas BoesenBirgit SchiøttSteffen SinningPoul NissenNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Lina Malinauskaite Saida Said Caglanur Sahin Julie Grouleff Azadeh Shahsavar Henriette Bjerregaard Pernille Noer Kasper Severinsen Thomas Boesen Birgit Schiøtt Steffen Sinning Poul Nissen A conserved leucine occupies the empty substrate site of LeuT in the Na+-free return state
description	Neurotransmitter:sodium symporters (NSS) perform Na+-dependent amino-acid uptake, but a full structural description of their function is lacking. Here the authors present a structure of the bacterial NSS LeuT in the outward-oriented empty state and show that a Leu residue occupies the empty substrate site and is essential for function.
format	article
author	Lina Malinauskaite Saida Said Caglanur Sahin Julie Grouleff Azadeh Shahsavar Henriette Bjerregaard Pernille Noer Kasper Severinsen Thomas Boesen Birgit Schiøtt Steffen Sinning Poul Nissen
author_facet	Lina Malinauskaite Saida Said Caglanur Sahin Julie Grouleff Azadeh Shahsavar Henriette Bjerregaard Pernille Noer Kasper Severinsen Thomas Boesen Birgit Schiøtt Steffen Sinning Poul Nissen
author_sort	Lina Malinauskaite
title	A conserved leucine occupies the empty substrate site of LeuT in the Na+-free return state
title_short	A conserved leucine occupies the empty substrate site of LeuT in the Na+-free return state
title_full	A conserved leucine occupies the empty substrate site of LeuT in the Na+-free return state
title_fullStr	A conserved leucine occupies the empty substrate site of LeuT in the Na+-free return state
title_full_unstemmed	A conserved leucine occupies the empty substrate site of LeuT in the Na+-free return state
title_sort	conserved leucine occupies the empty substrate site of leut in the na+-free return state
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/0c4dfaf71bb84eee82b29dd34e8c741a
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A conserved leucine occupies the empty substrate site of LeuT in the Na+-free return state

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