Structural highlights
Publication Abstract from PubMed
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.
Crystal structure of a substrate-free aspartate transporter.,Jensen S, Guskov A, Rempel S, Hanelt I, Slotboom DJ Nat Struct Mol Biol. 2013 Oct;20(10):1224-6. doi: 10.1038/nsmb.2663. Epub 2013, Sep 8. PMID:24013209[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jensen S, Guskov A, Rempel S, Hanelt I, Slotboom DJ. Crystal structure of a substrate-free aspartate transporter. Nat Struct Mol Biol. 2013 Oct;20(10):1224-6. doi: 10.1038/nsmb.2663. Epub 2013, Sep 8. PMID:24013209 doi:http://dx.doi.org/10.1038/nsmb.2663
