Maltose-binding protein

From Proteopedia

Contents 1 Function 2 Relevance 3 Structural highlights 4 3D structures of maltose-binding protein 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 The MBP sugar binding cleft is rich with protein-ligand hydrogen bonds[3]. Water molecules are shown as red spheres. 3D structures of maltose-binding protein Maltose-binding protein 3D structures

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References

1. ↑ 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
2. ↑ 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
3. ↑ Quiocho FA, Spurlino JC, Rodseth LE. Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor. Structure. 1997 Aug 15;5(8):997-1015. PMID:9309217