Structural highlights
Publication Abstract from PubMed
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 GltTk 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.
Coupled binding mechanism of three sodium ions and aspartate in the glutamate transporter homologue GltTk.,Guskov A, Jensen S, Faustino I, Marrink SJ, Slotboom DJ Nat Commun. 2016 Nov 10;7:13420. doi: 10.1038/ncomms13420. PMID:27830699[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Guskov A, Jensen S, Faustino I, Marrink SJ, Slotboom DJ. Coupled binding mechanism of three sodium ions and aspartate in the glutamate transporter homologue GltTk. Nat Commun. 2016 Nov 10;7:13420. doi: 10.1038/ncomms13420. PMID:27830699 doi:http://dx.doi.org/10.1038/ncomms13420
