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Crystal structure of a substrate-free aspartate transporter

Nature Structural & Molecular Biology volume 20, pages 1224–1226 (2013)Cite this article

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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.

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Figure 1: Aspartate-binding site.
Figure 2: Cation-binding sites.
Figure 3: Translocation cycle of archaeal aspartate transporters based on the available crystal structures.

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Acknowledgements

We thank B. Poolman and M. Jaehme for critically reading the manuscript and the European Synchrotron Radiation Facility for beamline access. This work was supported by the Deutsche Forschungsgemeinschaft (I.H.) (HA 6322/1-1), the Netherlands Organisation for Scientific Research (NWO vidi 700.54.423 and vici 865.11.001 grants to D.J.S.) and the European Union (EU EDICT program and European Research Council starting grant 282083 to D.J.S.).

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Author notes

  1. Sonja Jensen and Albert Guskov: These authors contributed equally to this work.

Authors and Affiliations

  1. Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, The Netherlands

    Sonja Jensen, Albert Guskov, Stephan Rempel, Inga Hänelt & Dirk Jan Slotboom

  2. Zernike Institute for Advanced Materials, University of Groningen, Groningen, The Netherlands

    Dirk Jan Slotboom

Authors
  1. Sonja Jensen
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  2. Albert Guskov
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Contributions

All authors designed experiments. I.H. constructed the expression vector. S.J., A.G. and S.R. performed all other experiments. S.J., A.G., S.R. and D.J.S. analyzed data. S.J., A.G. and D.J.S. wrote the manuscript.

Corresponding author

Correspondence to Dirk Jan Slotboom.

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The authors declare no competing financial interests.

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Supplementary Figures 1–5 and Supplementary Tables 1 and 2 (PDF 5907 kb)

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Jensen, S., Guskov, A., Rempel, S. et al. Crystal structure of a substrate-free aspartate transporter. Nat Struct Mol Biol 20, 1224–1226 (2013). https://doi.org/10.1038/nsmb.2663

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