Coupled binding mechanism of three sodium ions and aspartate in the glutamate transporter homologue GltTk.
Guskov, A., Jensen, S., Faustino, I., Marrink, S.J., Slotboom, D.J.(2016) Nat Commun 7: 13420-13420
- PubMed: 27830699 
- DOI: https://doi.org/10.1038/ncomms13420
- Primary Citation of Related Structures:  
5DWY, 5E9S - PubMed Abstract: 
Glutamate transporters catalyse the thermodynamically unfavourable transport of anionic amino acids across the cell membrane by coupling it to the downhill transport of cations. This coupling mechanism is still poorly understood, in part because the available crystal structures of these transporters are of relatively low resolution. Here we solve crystal structures of the archaeal transporter Glt Tk in the presence and absence of aspartate and use molecular dynamics simulations and binding assays to show how strict coupling between the binding of three sodium ions and aspartate takes place.
Organizational Affiliation: 
University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute, Nijenborgh 4, 9747 AG Groningen, The Netherlands.