L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction

L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction

L-Amino acid Transporters (LATs) are asymmetric amino acid exchangers. Here the authors determine the crystal structure of a prokaryotic LAT, the alanine-serine-cysteine exchanger (BasC) and identify key residues for asymmetric substrate interaction in both BasC and the homologous human transporter...

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Main Authors: Ekaitz Errasti-Murugarren, Joana Fort, Paola Bartoccioni, Lucía Díaz, Els Pardon, Xavier Carpena, Meritxell Espino-Guarch, Antonio Zorzano, Christine Ziegler, Jan Steyaert, Juan Fernández-Recio, Ignacio Fita, Manuel Palacín
Format: Article
Language:English
Published: Nature Publishing Group 2019-04-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-09837-z
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spelling doaj-02f00387781745f491d1d369e1db22152021-05-11T11:35:38ZengNature Publishing GroupNature Communications2041-17232019-04-0110111210.1038/s41467-019-09837-zL amino acid transporter structure and molecular bases for the asymmetry of substrate interactionEkaitz Errasti-Murugarren0Joana Fort1Paola Bartoccioni2Lucía Díaz3Els Pardon4Xavier Carpena5Meritxell Espino-Guarch6Antonio Zorzano7Christine Ziegler8Jan Steyaert9Juan Fernández-Recio10Ignacio Fita11Manuel Palacín12Institute for Research in Biomedicine (IRB Barcelona), Barcelona Institute of Science and TechnologyInstitute for Research in Biomedicine (IRB Barcelona), Barcelona Institute of Science and TechnologyInstitute for Research in Biomedicine (IRB Barcelona), Barcelona Institute of Science and TechnologyBarcelona Supercomputing Center (BSC), Joint BSC-CRG-IRB Research Program in Computational Biology, Life Sciences DepartmentVIB-VUB Center for Structural Biology, Pleinlaan 2CELLS-ALBA Synchrotron Light SourceTranslational Medicine, Sidra MedicineInstitute for Research in Biomedicine (IRB Barcelona), Barcelona Institute of Science and TechnologyInstitute of Biophysics and Biophysical Chemistry, Universität RegensburgVIB-VUB Center for Structural Biology, Pleinlaan 2Barcelona Supercomputing Center (BSC), Joint BSC-CRG-IRB Research Program in Computational Biology, Life Sciences DepartmentBarcelona Molecular Biology Institut (IBMB-CSIC) and Unit of Excellence María de MaeztuInstitute for Research in Biomedicine (IRB Barcelona), Barcelona Institute of Science and TechnologyL-Amino acid Transporters (LATs) are asymmetric amino acid exchangers. Here the authors determine the crystal structure of a prokaryotic LAT, the alanine-serine-cysteine exchanger (BasC) and identify key residues for asymmetric substrate interaction in both BasC and the homologous human transporter Asc-1 through functional studies.https://doi.org/10.1038/s41467-019-09837-z
collection DOAJ
language English
format Article
sources DOAJ
author Ekaitz Errasti-Murugarren
Joana Fort
Paola Bartoccioni
Lucía Díaz
Els Pardon
Xavier Carpena
Meritxell Espino-Guarch
Antonio Zorzano
Christine Ziegler
Jan Steyaert
Juan Fernández-Recio
Ignacio Fita
Manuel Palacín
spellingShingle Ekaitz Errasti-Murugarren
Joana Fort
Paola Bartoccioni
Lucía Díaz
Els Pardon
Xavier Carpena
Meritxell Espino-Guarch
Antonio Zorzano
Christine Ziegler
Jan Steyaert
Juan Fernández-Recio
Ignacio Fita
Manuel Palacín
L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction
Nature Communications
author_facet Ekaitz Errasti-Murugarren
Joana Fort
Paola Bartoccioni
Lucía Díaz
Els Pardon
Xavier Carpena
Meritxell Espino-Guarch
Antonio Zorzano
Christine Ziegler
Jan Steyaert
Juan Fernández-Recio
Ignacio Fita
Manuel Palacín
author_sort Ekaitz Errasti-Murugarren
title L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction
title_short L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction
title_full L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction
title_fullStr L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction
title_full_unstemmed L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction
title_sort l amino acid transporter structure and molecular bases for the asymmetry of substrate interaction
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2019-04-01
description L-Amino acid Transporters (LATs) are asymmetric amino acid exchangers. Here the authors determine the crystal structure of a prokaryotic LAT, the alanine-serine-cysteine exchanger (BasC) and identify key residues for asymmetric substrate interaction in both BasC and the homologous human transporter Asc-1 through functional studies.
url https://doi.org/10.1038/s41467-019-09837-z
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