Publication

Crystal structure of a substrate-free aspartate transporter

Jensen, S., Guskov, A., Rempel, S., Hänelt, I. & Slotboom, D. J., Oct-2013, In : Nature Structural & Molecular Biology. 20, 10, p. 1224-1226 3 p.

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DOI

Archaeal glutamate transporter homologs catalyze the coupled uptake of aspartate and three sodium ions. After the delivery of the substrate and sodium ions to the cytoplasm, the empty binding site must reorient to the outward-facing conformation to reset the transporter. Here, we report a crystal structure of the substrate-free transporter Glt(Tk) from Thermococcus kodakarensis, which provides insight into the mechanism of this essential step in the translocation cycle.

Original languageEnglish
Pages (from-to)1224-1226
Number of pages3
JournalNature Structural & Molecular Biology
Volume20
Issue number10
Publication statusPublished - Oct-2013

    Keywords

  • NEURONAL GLUTAMATE TRANSPORTER, PYROCOCCUS-HORIKOSHII, HOMOLOG, BINDING, SELECTIVITY, GLT(PH), MODEL, SITE
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