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
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/76bc5140efca4c9482b7af7a5ab080f1
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Sumario: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.