1XFH

Structure of glutamate transporter homolog from Pyrococcus horikoshii

Summary for 1XFH

• Entry DOI: 10.2210/pdb1xfh/pdb
• Descriptor: proton glutamate symport protein (1 entity in total)
• Functional Keywords: trimeric helical transmembrane protein, transport protein
• Biological source: Pyrococcus horikoshii
• Cellular location: Cell membrane {ECO:0000305|PubMed:15483603, ECO:0000305|PubMed:17230192, ECO:0000305|PubMed:17435767, ECO:0000305|PubMed:19380583, ECO:0000305|PubMed:28137870, ECO:0000305|Ref: O59010
• Total number of polymer chains: 3
• Total formula weight: 133925.83

Authors

Yernool, D.,Boudker, O.,Jin, Y.,Gouaux, E. (deposition date: 2004-09-14, release date: 2004-10-26, Last modification date: 2024-02-14)

Primary citation

Yernool, D.,Boudker, O.,Jin, Y.,Gouaux, E.
Structure of a glutamate transporter homologue from Pyrococcus horikoshii
Nature, 431:811-818, 2004

PubMed Abstract: Glutamate transporters are integral membrane proteins that catalyse the concentrative uptake of glutamate from the synapse to intracellular spaces by harnessing pre-existing ion gradients. In the central nervous system glutamate transporters are essential for normal development and function, and are implicated in stroke, epilepsy and neurodegenerative diseases. Here we present the crystal structure of a eukaryotic glutamate transporter homologue from Pyrococcus horikoshii. The transporter is a bowl-shaped trimer with a solvent-filled extracellular basin extending halfway across the membrane bilayer. At the bottom of the basin are three independent binding sites, each cradled by two helical hairpins, reaching from opposite sides of the membrane. We propose that transport of glutamate is achieved by movements of the hairpins that allow alternating access to either side of the membrane.

PubMed: 15483603
DOI: 10.1038/nature03018

Experimental method

X-RAY DIFFRACTION (3.5 Å)