Backbone chemical shifts assignments of D-allose binding protein in the free form and in complex with D-allose.
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).
Castaño
David
D
Structural Biology Unit, CICbioGUNE, Bizkaia Technology Park, Derio, Spain.
Millet
Oscar
O
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
D018528:ATP-Binding Cassette Transporters; C118436:D-allose binding protein, E coli; D029968:Escherichia coli Proteins; C002055:allose; D005947:Glucose