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

Lina Malinauskaite; Saida Said; Caglanur Sahin; Julie Grouleff; Azadeh Shahsavar; Henriette Bjerregaard; Pernille Noer; Kasper Severinsen; Thomas Boesen; Birgit Schiøtt; Steffen Sinning; Poul Nissen

doi:10.1038/ncomms11673

Nature Communications (May 2016)

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

Lina Malinauskaite,
Saida Said,
Caglanur Sahin,
Julie Grouleff,
Azadeh Shahsavar,
Henriette Bjerregaard,
Pernille Noer,
Kasper Severinsen,
Thomas Boesen,
Birgit Schiøtt,
Steffen Sinning,
Poul Nissen

Affiliations

Lina Malinauskaite: Department of Molecular Biology and Genetics, Danish Research Institute of Translational Neuroscience—DANDRITE, Nordic-EMBL Partnership for Molecular Medicine, Aarhus University
Saida Said: Department of Clinical Medicine, Translational Neuropsychiatry Unit, Aarhus University
Caglanur Sahin: Department of Molecular Biology and Genetics, Danish Research Institute of Translational Neuroscience—DANDRITE, Nordic-EMBL Partnership for Molecular Medicine, Aarhus University
Julie Grouleff: Department of Chemistry, inSPIN and iNANO centers, Aarhus University
Azadeh Shahsavar: Department of Molecular Biology and Genetics, Danish Research Institute of Translational Neuroscience—DANDRITE, Nordic-EMBL Partnership for Molecular Medicine, Aarhus University
Henriette Bjerregaard: Department of Clinical Medicine, Translational Neuropsychiatry Unit, Aarhus University
Pernille Noer: Department of Clinical Medicine, Translational Neuropsychiatry Unit, Aarhus University
Kasper Severinsen: Department of Clinical Medicine, Translational Neuropsychiatry Unit, Aarhus University
Thomas Boesen: Department of Molecular Biology and Genetics, Danish Research Institute of Translational Neuroscience—DANDRITE, Nordic-EMBL Partnership for Molecular Medicine, Aarhus University
Birgit Schiøtt: Department of Chemistry, inSPIN and iNANO centers, Aarhus University
Steffen Sinning: Department of Clinical Medicine, Translational Neuropsychiatry Unit, Aarhus University
Poul Nissen: Department of Molecular Biology and Genetics, Danish Research Institute of Translational Neuroscience—DANDRITE, Nordic-EMBL Partnership for Molecular Medicine, Aarhus University

DOI: https://doi.org/10.1038/ncomms11673
Journal volume & issue: Vol. 7, no. 1
pp. 1 – 11

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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