| Literature DB >> 24013209 |
Sonja Jensen1, Albert Guskov, Stephan Rempel, Inga Hänelt, Dirk Jan Slotboom.
Abstract
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 GltTk from Thermococcus kodakarensis, which provides insight into the mechanism of this essential step in the translocation cycle.Entities:
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Year: 2013 PMID: 24013209 DOI: 10.1038/nsmb.2663
Source DB: PubMed Journal: Nat Struct Mol Biol ISSN: 1545-9985 Impact factor: 15.369