Molecular Playground/RBP
From Proteopedia
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== Molecular Playground/D-Ribose Binding Protein == | == Molecular Playground/D-Ribose Binding Protein == | ||
| - | <Structure load='1urp' size=' | + | <Structure load='1urp' size='350' frame='true' align='right' caption='Tetrameric open conformation of E. Coli D-Ribose Binding Protein for signal transduction of Chemotaxis machinery RBP [[1urp]]. The differnt colors signify the different subunits.' scene='Insert optional scene name here' /> |
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. See the figure to the right. | 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. See the figure to the right. | ||
Current revision
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.
Molecular Playground/D-Ribose Binding Protein
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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. See the figure to the right.
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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.
Molecular Playground banner: A bacterial periplasmic ligand-binding protein for chemotaxis signal transduction.
