Molecular Playground/Bacterial Chemotaxis Complex
From Proteopedia
| Line 7: | Line 7: | ||
===Structure=== | ===Structure=== | ||
| - | The <scene name='57/571407/Cytoplasmic_receptor/1'> | + | • The <scene name='57/571407/Cytoplasmic_receptor/1'>chemoreceptor</scene> (1QU7) – 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 where both CheW and CheA interact and bind. |
| + | |||
| + | • CheA is a large 5-subdomain (P1-P5) histidine kinase that auto-phosphorylates depending on it's interaction with the receptor and localized concentrations of the response regulator protein CheY. | ||
Revision as of 20:50, 16 December 2013
ö
|
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.
Structure
• The (1QU7) – also called methyl-accepting protein, MCP – is a ~380Å long, alpha helical homo-dimer with many domains. The at the cytosplasmic tip is where both CheW and CheA interact and bind.
• CheA is a large 5-subdomain (P1-P5) histidine kinase that auto-phosphorylates depending on it's interaction with the receptor and localized concentrations of the response regulator protein CheY.
