User:Jan Panteli/sandbox 1

From Proteopedia

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D- Ribose Binding Protein (RBP) is involved in signal transduction of the chemokine D-ribose to stimulate chemotaxis in 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 as a tetramer with four identical domains, A,B,C,and D. Within each of these domains lies a binding site for d-ribose.

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

When d-ribose enters the periplasmic space of the gram negative bacteria and binds to one of the monomers, the RBP monomer undergoes a conformational change and folds in a hinge motion locking the ligand into its

. The ligand bound form of the RBP 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.