Coupled binding mechanism of three sodium ions and aspartate in the glutamate transporter homologue GltTk

Albert Guskov, Sonja Jensen, Ignacio Faustino, Siewert J. Marrink and Dirk Jan Slotboom ()
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Albert Guskov: University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute
Sonja Jensen: University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute
Ignacio Faustino: University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute
Siewert J. Marrink: University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute
Dirk Jan Slotboom: University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute

Nature Communications, 2016, vol. 7, issue 1, 1-6

Abstract: 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 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.

Date: 2016
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13420

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DOI: 10.1038/ncomms13420

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