Kinetic mechanism of Na+-coupled aspartate transport catalyzed by GltTk

Trinco et al. measure aspartate uptake rates in proteoliposomes containing purified prokaryotic Na+-coupled aspartate transporter GltTk. To overcome limitation of protein orientation, they use synthetic nanobody that blocks transporters from outside and reveal mechanistic features of Na+-aspartate s...

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Autores principales: Gianluca Trinco, Valentina Arkhipova, Alisa A. Garaeva, Cedric A. J. Hutter, Markus A. Seeger, Albert Guskov, Dirk J. Slotboom
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Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/76bc5140efca4c9482b7af7a5ab080f1
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spelling oai:doaj.org-article:76bc5140efca4c9482b7af7a5ab080f12021-12-02T16:04:30ZKinetic mechanism of Na+-coupled aspartate transport catalyzed by GltTk10.1038/s42003-021-02267-y2399-3642https://doaj.org/article/76bc5140efca4c9482b7af7a5ab080f12021-06-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-02267-yhttps://doaj.org/toc/2399-3642Trinco et al. measure aspartate uptake rates in proteoliposomes containing purified prokaryotic Na+-coupled aspartate transporter GltTk. To overcome limitation of protein orientation, they use synthetic nanobody that blocks transporters from outside and reveal mechanistic features of Na+-aspartate symport that cannot be observed in detergent solution.Gianluca TrincoValentina ArkhipovaAlisa A. GaraevaCedric A. J. HutterMarkus A. SeegerAlbert GuskovDirk J. SlotboomNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-11 (2021)
institution DOAJ
collection DOAJ
language EN
topic Biology (General)
QH301-705.5
spellingShingle Biology (General)
QH301-705.5
Gianluca Trinco
Valentina Arkhipova
Alisa A. Garaeva
Cedric A. J. Hutter
Markus A. Seeger
Albert Guskov
Dirk J. Slotboom
Kinetic mechanism of Na+-coupled aspartate transport catalyzed by GltTk
description Trinco et al. measure aspartate uptake rates in proteoliposomes containing purified prokaryotic Na+-coupled aspartate transporter GltTk. To overcome limitation of protein orientation, they use synthetic nanobody that blocks transporters from outside and reveal mechanistic features of Na+-aspartate symport that cannot be observed in detergent solution.
format article
author Gianluca Trinco
Valentina Arkhipova
Alisa A. Garaeva
Cedric A. J. Hutter
Markus A. Seeger
Albert Guskov
Dirk J. Slotboom
author_facet Gianluca Trinco
Valentina Arkhipova
Alisa A. Garaeva
Cedric A. J. Hutter
Markus A. Seeger
Albert Guskov
Dirk J. Slotboom
author_sort Gianluca Trinco
title Kinetic mechanism of Na+-coupled aspartate transport catalyzed by GltTk
title_short Kinetic mechanism of Na+-coupled aspartate transport catalyzed by GltTk
title_full Kinetic mechanism of Na+-coupled aspartate transport catalyzed by GltTk
title_fullStr Kinetic mechanism of Na+-coupled aspartate transport catalyzed by GltTk
title_full_unstemmed Kinetic mechanism of Na+-coupled aspartate transport catalyzed by GltTk
title_sort kinetic mechanism of na+-coupled aspartate transport catalyzed by glttk
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/76bc5140efca4c9482b7af7a5ab080f1
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AT cedricajhutter kineticmechanismofnacoupledaspartatetransportcatalyzedbyglttk
AT markusaseeger kineticmechanismofnacoupledaspartatetransportcatalyzedbyglttk
AT albertguskov kineticmechanismofnacoupledaspartatetransportcatalyzedbyglttk
AT dirkjslotboom kineticmechanismofnacoupledaspartatetransportcatalyzedbyglttk
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