Molecular Playground/Bacterial Chemotaxis Complex: Difference between revisions
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<applet load='3UR1' size='400' color='white' frame='true' align='right' caption='A single asymmetric unit ternary complex with the truncated receptor, CheA, and CheW [[3UR1]]' scene='57/571407/Single_ternary_complex/1'/> | ö<applet load='3UR1' size='400' color='white' frame='true' align='right' caption='A single asymmetric unit ternary complex with the truncated receptor, CheA, and CheW [[3UR1]]' scene='57/571407/Single_ternary_complex/1'/> | ||
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. | 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. | ||
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===Structure=== | ===Structure=== | ||
The transmembrane chemoreceptor (also called methyl-accepting protein, MCP) is a ~380Å long, alpha helical homo-dimer with many domains. The signaling domain at the cytosplasmic tip is both CheW and CheA interact and bind. | The <scene name='57/571407/Cytoplasmic_receptor/1'>transmembrane chemoreceptor</scene> (also called methyl-accepting protein, MCP) is a ~380Å long, alpha helical homo-dimer with many domains. The <scene name='57/571407/Cytoplasmic_receptor/2'>signaling domain</scene> at the cytosplasmic tip is both CheW and CheA interact and bind. | ||
Revision as of 23:36, 16 December 2013
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One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst.
Bacterial chemotaxis is a method for cells to sense and adapt to chemicals in their environment. It is carried out by large arrays of membrane associated multi-protein complexes that form at the poles of the cells. The major players involved are the transmembrane receptor, histidine kinase CheA, and scaffold/adaptor protein CheW. Repellants and attractants bind to the periplasmic domain of the receptor. The signal is then relayed within the cytoplasm to govern CheA's kinase activity, and ultimately lead to changes in swimming behavior.
StructureStructure
The (also called methyl-accepting protein, MCP) is a ~380Å long, alpha helical homo-dimer with many domains. The at the cytosplasmic tip is both CheW and CheA interact and bind.