Na+:Aspartate Coupling Stoichiometry in the Glutamate Transporter Homologue GltPh

Biochemistry ◽  
2010 ◽  
Vol 49 (17) ◽  
pp. 3511-3513 ◽  
Author(s):  
Maarten Groeneveld ◽  
Dirk-Jan Slotboom
eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Valentina Arkhipova ◽  
Gianluca Trinco ◽  
Thijs W Ettema ◽  
Sonja Jensen ◽  
Dirk J Slotboom ◽  
...  

Mammalian glutamate transporters are crucial players in neuronal communication as they perform neurotransmitter reuptake from the synaptic cleft. Besides L-glutamate and L-aspartate, they also recognize D-aspartate, which might participate in mammalian neurotransmission and/or neuromodulation. Much of the mechanistic insight in glutamate transport comes from studies of the archeal homologs GltPh from Pyrococcus horikoshii and GltTk from Thermococcus kodakarensis. Here, we show that GltTk transports D-aspartate with identical Na+: substrate coupling stoichiometry as L-aspartate, and that the affinities (Kd and Km) for the two substrates are similar. We determined a crystal structure of GltTk with bound D-aspartate at 2.8 Å resolution. Comparison of the L- and D-aspartate bound GltTk structures revealed that D-aspartate is accommodated with only minor rearrangements in the structure of the binding site. The structure explains how the geometrically different molecules L- and D-aspartate are recognized and transported by the protein in the same way.


2001 ◽  
Vol 13 (1) ◽  
pp. 119-128 ◽  
Author(s):  
Vemuganti L. Raghavendra Rao ◽  
Aclan Dogan ◽  
Kellie K. Bowen ◽  
Kathryn G. Todd ◽  
Robert J. Dempsey

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