The periplasmic-binding component of ABC transport systems specific for maltose and related oligosaccharides; possess type 2 periplasmic binding fold.
This family represents the periplasmic binding component of ABC transport systems involved in uptake of oligosaccharides including maltose, trehalose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Feature 1:chemical substrate binding site [chemical binding site]
Evidence:
Structure:1URD; the maltose-maltodextrin Binding protein of the thermoacidophilic bacterium Alicyclobacillus acidocaldarius in complex with maltotriose, contacts at 4A.
Structure:1EU8; trehalose/maltose-binding protein from the hyperthermophilic archaeon Thermococcus litoralis in complex with trehalose, contacts at 4A.
Jiyao W et al.(2023). "The conserved domain database in 2023.",