User:Jan Panteli/sandbox 1

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== Exploring the Structure ==
== Exploring the Structure ==
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<Structure load='1urp' size='500' frame='true' align='right' caption='Open Conformation of E. Coli D-Ribose Binding Protein for signal transduction of Chemotaxis machinery RBP(1URP)' scene='Insert optional scene name here' />
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<Structure load='1urp' size='500' frame='true' align='right' caption='Tetrameric open conformation of E. Coli D-Ribose Binding Protein for signal transduction of Chemotaxis machinery RBP(1URP)' scene='Insert optional scene name here' />
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There are four domains to RBP, A,B,C,and D. These domains form a binding site for d-ribose and the bound form of the protein then interacts with transmembrane protein Trg, the chemotaxis transducer for d-ribose.
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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.
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<Structure load='2dri' size='500' frame='true' align='right' caption='Closed conformation of the RBP upon binding with ligand, D-Ribose in Domain A' scene='Insert optional scene name here' />
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<Structure load='2dri' size='500' frame='true' align='right' caption='Closed conformation of the RBP upon binding with ligand (2dri), D-Ribose in monomer' scene='Insert optional scene name here' />
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<Structure load='Insert PDB code or filename here' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Revision as of 18:59, 4 May 2011

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

Tetrameric open conformation of E. Coli D-Ribose Binding Protein for signal transduction of Chemotaxis machinery RBP(1URP)

Drag the structure with the mouse to rotate

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.

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

Drag the structure with the mouse to rotate

Insert caption here

Drag the structure with the mouse to rotate

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Jan Panteli

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