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Explore the structure, interactions, and function of Maltodextrin Binding Protein (MBP), an integral membrane protein involved in maltose transport and chemotaxis system in E. coli. Learn about its topology, hydrogen bonding, van der Waals interactions, structural plasticity, specificity, and sites interacting with membrane transport and chemotaxis.
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Maltodextrin Binding Protein Seena Koshy
Maltodextrin Binding Protein (MBP) • Belongs to the ATP binding casette (ABC) of active transport system. A model for maltose transport in E. coli: MalF and MalG are integral membrane proteins MalK is the ATP-binding protein
3MBP 1OMP
Ligands • PhysiologicalNon-physiological Maltose Maltotetraose Cyclodextrin Maltotriose
Outline of my Pymol presentation • 1. Topology of the Structure • 2. Hydrogen Bond interaction cooperative hydrogen bonding Intersugar hydrogen bonding • 3. Van der Waals interaction • aromatic stacking • 4. Structural Plasticity hinge bending between two domain oligosaccharide induced conformational change • 5. Specificity • 6. Sites interacting with Membrane transport • 7. Sites interacting with the Chemotaxis system