title: Backbone chemical shifts assignments of D-allose binding protein in the free form and in complex with D-allose.
abstract: D-allose binding protein (ALBP) belongs to the family of perisplamic receptors of the bacterial ABC transporter system. ALBP experiences a significant conformational rearrangement upon binding to the sugar. Here, we report the sequential backbone assignment for the ALBP from Escherichia coli in the free form (BMRB no. 16982) and in complex with D-allose (BMRB no. 16984).
authors: Structural Biology Unit, CICbioGUNE, Bizkaia Technology Park, Derio, Spain.
authors: David
authors: D
authors: Castaño
authors: Oscar
authors: O
authors: Millet
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D005947:Glucose / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D013696:Temperature
chemical_list: D018528:ATP-Binding Cassette Transporters; C118436:D-allose binding protein, E coli; D029968:Escherichia coli Proteins; C002055:allose; D005947:Glucose