Plenary Lecture
Structure, Dynamics and Thermodynamics of a Glutamate Transporter Homologue

Glutamate transporters are responsible for clearance of the neurotransmitter glutamate from the synaptic cleft following rounds of neurotransmission. They maintain steep concentration gradients of glutamate by coupling its uptake to symport of sodium ions and protons and to antiport of potassium ions. We have been investigating the molecular mechanism of this family of transporters using an archaeal homologue GltPh as a model system. For GltPh, we obtained the crystal structures of key states along the transport cycle, and also probed the dynamics and thermodynamics that define the rates of substrate uptake and the mechanism of coupling the uptake to movements of ions.