User:Jan Panteli/sandbox 1
From Proteopedia
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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' /> | <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' /> | ||
| - | 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 | + | 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 <scene name='User:Jan_Panteli/sandbox_1/Rbp_bound_to_d-ribose/1'>binds</scene> to one of the monomers, the 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. |
<Structure load='2dri' size='500' frame='true' align='right' caption='Closed monomeric conformation of the RBP upon binding with ligand (2dri), D-Ribose' scene='Insert optional scene name here' /> | <Structure load='2dri' size='500' frame='true' align='right' caption='Closed monomeric conformation of the RBP upon binding with ligand (2dri), D-Ribose' scene='Insert optional scene name here' /> | ||
Revision as of 19:28, 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
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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 to one of the monomers, the 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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