User:Jan Panteli/sandbox 1

From Proteopedia

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E. Coli D- Ribose Binding Protein (RBP) is involved in signal transduction of the chemokine D-ribose to stimulate chemotaxis in the bacteria.

One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.

Exploring the Structure

spinqualitylabelsall models Tetrameric open conformation of E. Coli D-Ribose Binding Protein for signal transduction of Chemotaxis machinery RBP(1URP) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

In the open conformation the RBP is found in a tetramer four identical domains, A,B,C,and D. Within each of these domains lies a binding site for d-ribose. When d-ribose enters the periplasmic space of the gram negative bacteria and binds to one of the monomers this bound form then interacts with transmembrane protein Trg, the chemotaxis transducer for d-ribose. Trg then sends biochemical signals to tell the bacteria's flagella to rotate leading to bacterial migration towards the sugar food source.

spinqualitylabelsall models Closed conformation of the RBP upon binding with ligand (2dri), D-Ribose in monomer Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

spinqualitylabelsall models Insert caption here Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image