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BIO DESIGN

pISSN 2288-6982
eISSN 2288-7105

Article

Article

Mini review

BioDesign 2020; 8(4): 73-82

Published online December 30, 2020

https://doi.org/10.34184/kssb.2020.8.4.73

© Korean Society for Structural Biology

Structural understanding of the transport cycle of glutamate transporters

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: xiw2013@med.cornell.edu

Received: November 24, 2020; Revised: December 19, 2020; Accepted: December 20, 2020

Abstract

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.