Function
Maltose-binding protein (MBP) or ABC maltose transporter is part of the maltose/maltodextrin system in E. coli which is responsible of the catabolism of maltodextrin. MBP binds maltodextrin when the latter diffuses into the periplasm and passes it to proteins involved in active transport[1].
Relevance
MBP is widely used in molecular biology as it adds to the solubility of the proteins expressed in E. coli by being fused to them. The MBP-fusion protein can be purified by binding it to an amylose column followed by elution with maltose[2].
Structural highlights
3D structures of maltose-binding protein
Updated on 17-April-2016
References
- ↑ Kapust RB, Waugh DS. Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci. 1999 Aug;8(8):1668-74. PMID:10452611 doi:http://dx.doi.org/10.1110/ps.8.8.1668
- ↑ Sun P, Tropea JE, Waugh DS. Enhancing the solubility of recombinant proteins in Escherichia coli by using hexahistidine-tagged maltose-binding protein as a fusion partner. Methods Mol Biol. 2011;705:259-74. doi: 10.1007/978-1-61737-967-3_16. PMID:21125392 doi:http://dx.doi.org/10.1007/978-1-61737-967-3_16
