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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2019-04-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-019-09837-z |
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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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