title: A molecular basis for tungstate selectivity in prokaryotic ABC transport systems.
abstract: The essential trace compounds tungstate and molybdate are taken up by cells via ABC transporters. Despite their similar ionic radii and chemical properties, the WtpA protein selectively binds tungstate in the presence of molybdate. Using site-directed mutagenesis of conserved binding pocket residues, we established a molecular basis for tungstate selectivity.
authors.affiliation: Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands.
authors.forename: Loes E
authors.initials: LE
authors.lastname: Bevers
authors.forename: Guenter
authors.initials: G
authors.lastname: Schwarz
authors.forename: Wilfred R
authors.initials: WR
authors.lastname: Hagen
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D019943:Amino Acid Substitution / Q000235:genetics; D008958:Models, Molecular; D008982:Molybdenum / Q000378:metabolism; D016297:Mutagenesis, Site-Directed; D050505:Mutant Proteins / Q000235:genetics / Q000378:metabolism; D020027:Pyrococcus furiosus / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity; D017973:Tungsten Compounds / Q000378:metabolism*
chemical_list: D018528:ATP-Binding Cassette Transporters; D050505:Mutant Proteins; D017973:Tungsten Compounds; C044659:molybdate; D008982:Molybdenum; C045951:tungstate