Molecular Playground/CheR: Difference between revisions
New page: One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at th... |
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<applet load='1bc5' size='[450,338]' frame='true' align='right' | <applet load='1bc5' size='[450,338]' frame='true' align='right' | ||
caption='S. typhimurium CheR | caption='S. typhimurium CheR [[1bc5]]' scene='User:Miaomin_Zhang/Sandbox_1/Revolutionary_conservation/7'/> | ||
CheR binds to a specific sequence at the C-termini of chemoreceptors through noncovalent interactions like hydrogen bonds and methylates neighboring receptor molecules. The <scene name='User:Miaomin_Zhang/Sandbox_1/Revolutionary_conservation/7'>3D structure</scene> on the right shows the S. typhimurium CheR protein in revolutionary conservation grade colors [[http://proteopedia.org/wiki/index.php/Conservation%2C_Evolutionary]]. The green chain represents the C-terminal pentapeptide of the aspartate receptor (Tar) to which CheR is attached; and the methylation reaction product, S-adenosylhomocysteine (AdoHcy) that lies at center of CheR is shown in ball-and-stick model and CPK element colors. As seen from this scene, the active site of CheR is the most highly conserved part of the protein. | CheR binds to a specific sequence at the C-termini of chemoreceptors through noncovalent interactions like hydrogen bonds and methylates neighboring receptor molecules. The <scene name='User:Miaomin_Zhang/Sandbox_1/Revolutionary_conservation/7'>3D structure</scene> on the right shows the S. typhimurium CheR protein in revolutionary conservation grade colors [[http://proteopedia.org/wiki/index.php/Conservation%2C_Evolutionary]]. The green chain represents the C-terminal pentapeptide of the aspartate receptor (Tar) to which CheR is attached; and the methylation reaction product, S-adenosylhomocysteine (AdoHcy) that lies at center of CheR is shown in ball-and-stick model and CPK element colors. As seen from this scene, the active site of CheR is the most highly conserved part of the protein. | ||