title: Crystal structure of a substrate-free aspartate transporter.
abstract: Archaeal glutamate transporter homologs catalyze the coupled uptake of aspartate and three sodium ions. After the delivery of the substrate and sodium ions to the cytoplasm, the empty binding site must reorient to the outward-facing conformation to reset the transporter. Here, we report a crystal structure of the substrate-free transporter GltTk from Thermococcus kodakarensis, which provides insight into the mechanism of this essential step in the translocation cycle.
authors.affiliation: 1] Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, The Netherlands. [2].
authors.forename: Sonja
authors.initials: S
authors.lastname: Jensen
authors.forename: Albert
authors.initials: A
authors.lastname: Guskov
authors.forename: Stephan
authors.initials: S
authors.lastname: Rempel
authors.forename: Inga
authors.initials: I
authors.lastname: Hänelt
authors.forename: Dirk Jan
authors.initials: DJ
authors.lastname: Slotboom
mesh_terms: D001224:Aspartic Acid / Q000378:metabolism*; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D013379:Substrate Specificity
chemical_list: D002352:Carrier Proteins; D001224:Aspartic Acid