Solution Structure of a Complex of the Histidine Autokinase CheA with Its Substrate CheY
| Autor: | Tetsuya Kawamura, Guoya Mo, Frederick W. Dahlquist, Hongjun Zhou |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
Models
Molecular Histidine Kinase Methyl-Accepting Chemotaxis Proteins Biology medicine.disease_cause Biochemistry Article Domain (software engineering) HAMP domain Bacterial Proteins medicine Nuclear Magnetic Resonance Biomolecular Escherichia coli Histidine Escherichia coli Proteins Membrane Proteins Chemotaxis Protein Structure Tertiary Kinetics Response regulator Spectrometry Fluorescence Cytoplasm Biophysics bacteria Phosphorylation biological phenomena cell phenomena and immunity Protein Kinases |
| Zdroj: | Biochemistry. 51:3786-3798 |
| ISSN: | 1520-4995 0006-2960 |
| Popis: | In the bacterial chemotaxis two-component signaling system, the histidine-containing phosphotransfer domain (the "P1" domain) of CheA receives a phosphoryl group from the catalytic domain (P4) of CheA and transfers it to the cognate response regulator (RR) CheY, which is docked by the P2 domain of CheA. Phosphorylated CheY then diffuses into the cytoplasm and interacts with the FliM moiety of the flagellar motors, thereby modulating the direction of flagellar rotation. Structures of various histidine phosphotransfer domains (HPt) complexed with their cognate RR domains have been reported. Unlike the Escherichia coli chemotaxis system, however, these systems lack the additional domains dedicated to binding to the response regulators, and the interaction of an HPt domain with an RR domain in the presence of such a domain has not been examined on a structural basis. In this study, we used modern nuclear magnetic resonance techniques to construct a model for the interaction of the E. coli CheA P1 domain (HPt) and CheY (RR) in the presence of the CheY-binding domain, P2. Our results indicate that the presence of P2 may lead to a slightly different relative orientation of the HPt and RR domains versus those seen in such complex structures previously reported. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|