The solution structure and interactions of CheW from Thermotoga maritima
Abstract
Using protein from the hyperthermophile Thermotoga maritima, we have determined the solution structure of CheW, an essential component in the formation of the bacterial chemotaxis signaling complex. The overall fold is similar to the regulatory domain of the chemotaxis kinase CheA. In addition, interactions of CheW with CheA were monitored by nuclear magnetic resonance (NMR) techniques. The chemical shift perturbation data show the probable contacts that CheW makes with CheA. In combination with previous genetic data, the structure also suggests a possible binding site for the chemotaxis receptor. These results provide a structural basis for a model in which CheW acts as a molecular bridge between CheA and the cytoplasmic tails of the receptor.
Additional Information
© 2002 Nature Publishing Group. Received 3 October 2001; Accepted 12 December 2001; Published online: 22 January 2002. Competing interests statement: The authors declare that they have no competing financial interests.Additional details
- Eprint ID
- 56428
- DOI
- 10.1038/nsb753
- Resolver ID
- CaltechAUTHORS:20150407-123014690
- Created
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2015-04-07Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field