BioDesign 2020; 8(4): 73-82
Published online December 30, 2020
© Korean Society for Structural Biology
Xiaoyu Wang1,* and SeCheol Oh2
1Department of Physiology and Biophysics, Weill Cornell Medicine, New York, NY 10065, USA
2Structural Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA
Correspondence to: email@example.com
Since the determination of the first crystal structure of a glutamate transporter homolog GltPh 16 years ago, the structural biology of glutamate transporter has progressed remarkably. To understand the complicated transport cycle of ion-coupled glutamate transport, each state’s high-resolution structural information in the transport cycle is essential. Many of the structural information and insights about the sodium-coupled symport mechanism were gained from structural studies of prokaryotic homologs sodium-aspartate symporters, GltPh and GltTk. Moreover, further insights were gained from recently unveiled structures of mammalian glutamate transporters (EAATs). Here we review GltPh, GltTk, and mammalian glutamate transporters’ structures and discuss how they help us to understand the ion-coupled transport mechanism in glutamate transporters.