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Structure of glutamate transporter homolog from Pyrococcus horikoshiiStructure of glutamate transporter homolog from Pyrococcus horikoshii
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGlutamate 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. Structure of a glutamate transporter homologue from Pyrococcus horikoshii.,Yernool D, Boudker O, Jin Y, Gouaux E Nature. 2004 Oct 14;431(7010):811-8. PMID:15483603[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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