| Primary Identifier | IPR006060 | Type | Family |
| Short Name | Maltose/Cyclodextrin-bd |
| description | Bacterial high affinity transport systems are involved in active transport of solutes across the cytoplasmic membrane. Most of the bacterial ABC (ATP-binding cassette) importers are composed of one or two transmembrane permease proteins, one or two nucleotide-binding proteins and a highly specific periplasmic solute-binding protein. In Gram-negative bacteria the solute-binding proteins are dissolved in the periplasm, while in archaea and Gram-positive bacteria, their solute-binding proteins are membrane-anchored lipoproteins [, ].This entry includes maltodextrin binding proteins and cyclodextrin-binding proteins (also known as galactooligosaccharide-binding proteins) from bacteria and archaea.Maltodextrin binding protein (MBP) is the primary component of bacterial high-affinity active transport and chemotaxis []. It is a monomeric protein, with 2 globular domains separated by a 2- or 3-stranded hinge. MBP binds and transports linear oligosaccharides (of up to 7 glucosyl units), as well as 2 cyclic maltodextrins which, although binding tightly, cannot be transported nor initiate a chemotactic response []. It is thought that the hinge region is critical for the correct functioning of MBP, not just in the binding and recognition of sugars,but also in allowing and maintaining the integrity of initiation of both active transport and chemotaxis [].The cyclodextrin-binding protein CYCB (also known as galactooligosaccharide-binding protein GANS) from Bacillus subtilis has been characterised. It is part of the ABC transporter complex GanPQS involved in the uptake of galactooligosaccharides and it has a role in galactan degradation [, ]. |
