User:Jan Panteli/sandbox 1

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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.
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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<Structure load='2dri' size='300' frame='true' align='bottom' caption='Closed monomeric conformation of the RBP upon binding with ligand (2dri), D-Ribose' scene='Insert optional scene name here' />
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<Structure load='2dri' size='300' frame='true' align='bottom' caption='Closed monomeric conformation of the RBP upon binding with ligand, D-Ribose(2dri)' scene='Insert optional scene name here' />
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 <scene name='User:Jan_Panteli/sandbox_1/Rbp_bound_to_d-ribose/1'>binding site</scene>.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.
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 <scene name='User:Jan_Panteli/sandbox_1/Rbp_bound_to_d-ribose/1'>binding site</scene>.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.

Revision as of 20:22, 4 May 2011

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

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.

Drag the structure with the mouse to rotate

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.

Closed monomeric conformation of the RBP upon binding with ligand, D-Ribose(2dri)

Drag the structure with the mouse to rotate

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.

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Jan Panteli

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