Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 20, Issue 10, Pages 1224-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2663
Keywords
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Funding
- Deutsche Forschungsgemeinschaft [HA 6322/1-1]
- Netherlands Organisation for Scientific Research [NWO vidi 700.54.423, vici 865.11.001]
- European Union (EU EDICT program and European Research Council starting grant) [282083]
- European Research Council (ERC) [282083] Funding Source: European Research Council (ERC)
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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.
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